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2',3'-dideoxy-ATP + H2O
2',3'-dideoxy-ADP + phosphate
-
53% of the phosphohydrolase activity with ATP
-
-
?
2',3'-dideoxy-GTP + H2O
2',3'-dideoxy-GDP + phosphate
-
28% of the phosphohydrolase activity with ATP
-
-
?
2'-deoxy-ATP + H2O
2'-deoxy-ADP + phosphate
-
62% of the phosphohydrolase activity with ATP
-
-
?
2'-deoxy-GTP + H2O
2'-deoxy-GDP + phosphate
-
39% of the phosphohydrolase activity with ATP
-
-
?
2'-deoxy-L-GTP + H2O
2'-deoxy-L-GDP + phosphate
-
11% of the phosphohydrolase activity with ATP
-
-
?
2'-fluoro-2'-deoxy-ATP + H2O
2'-fluoro-2'-deoxy-ADP + phosphate
-
63% of the phosphohydrolase activity with ATP
-
-
?
2'-fluoro-2'-deoxy-GTP + H2O
2'-fluoro-2'-deoxy-GDP + phosphate
-
22% of the phosphohydrolase activity with ATP
-
-
?
2'-O-methyl-GTP + H2O
2'-O-methyl-GDP + phosphate
-
24% of the phosphohydrolase activity with ATP
-
-
?
2-amino-ATP + H2O
2-amino-ADP + phosphate
-
103% of the phosphohydrolase activity with ATP
-
-
?
2-hydroxy-ATP + H2O
2-hydroxy-ADP + phosphate
-
40% of the phosphohydrolase activity with ATP
-
-
?
3'-deoxy-ATP + H2O
3'-deoxy-ADP + phosphate
-
60% of the phosphohydrolase activity with ATP
-
-
?
3'-deoxy-GTP + H2O
3'-deoxy-GDP + phosphate
-
12% of the phosphohydrolase activity with ATP
-
-
?
3'-O-methyl-GTP + H2O
3'-O-methyl-GDP + phosphate
-
35% of the phosphohydrolase activity with ATP
-
-
?
6-methyl-thio-GTP + H2O
6-methyl-thio-GDP + phosphate
-
40% of the phosphohydrolase activity with ATP
-
-
?
6-methyl-thio-ITP + H2O
6-methyl-thio-IDP + phosphate
-
16% of the phosphohydrolase activity with ATP
-
-
?
6-thio-GTP + H2O
6-thio-GDP + phosphate
-
93% of the phosphohydrolase activity with ATP
-
-
?
7-methyl-GTP + H2O
7-methyl-GDP + phosphate
-
14% of the phosphohydrolase activity with ATP
-
-
?
8-bromo-ATP + H2O
8-bromo-ADP + phosphate
-
124% of the phosphohydrolase activity with ATP
-
-
?
8-bromo-GTP + H2O
8-bromo-GDP + phosphate
-
19% of the phosphohydrolase activity with ATP
-
-
?
8-iodo-GTP + H2O
8-iodo-GDP + phosphate
-
54% of the phosphohydrolase activity with ATP
-
-
?
ara-ATP + H2O
ara-ADP + phosphate
-
18% of the phosphohydrolase activity with ATP
-
-
?
ATP + H2O
ADP + phosphate
CTP + H2O
CDP + phosphate
dATP + H2O
dADP + phosphate
dCTP + H2O
dCDP + phosphate
helicase activity is about 25% of the activity with ATP
-
-
?
dGTP + H2O
dGDP + phosphate
helicase activity is about 10% of the activity with ATP
-
-
?
dTTP + H2O
dTDP + phosphate
helicase activity is about 55% of the activity with ATP
-
-
?
GTP + H2O
GDP + phosphate
ITP + H2O
IDP + phosphate
-
49% of the phosphohydrolase activity with ATP
-
-
?
N1-methyl-ATP + H2O
N1-methyl-ADP + phosphate
-
66% of the phosphohydrolase activity with ATP
-
-
?
N1-methyl-GTP + H2O
N1-methyl-GDP + phosphate
-
49% of the phosphohydrolase activity with ATP
-
-
?
N6-methyl-ATP + H2O
N6-methyl-ADP + phosphate
-
43% of the phosphohydrolase activity with ATP
-
-
?
O6-methyl-GTP + H2O
O6-methyl-GDP + phosphate
-
17% of the phosphohydrolase activity with ATP
-
-
?
ribavirin triphosphate + H2O
ribavirin diphosphate + phosphate
-
36% of the phosphohydrolase activity with ATP
-
-
?
UTP + H2O
UDP + phosphate
XTP + H2O
XDP + phosphate
-
40% of the phosphohydrolase activity with ATP
-
-
?
additional information
?
-
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
cooperative binding of ATP and RNA leads to a compact helicase structure
-
-
?
ATP + H2O
ADP + phosphate
-
NTPase activity
-
-
?
ATP + H2O
ADP + phosphate
EF409381
-
-
-
?
ATP + H2O
ADP + phosphate
EF409381
either ATP or dATP is required for the unwinding activity
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
helicase activity requires the substrates possessing a 3' un-base-paired region on the RNA template strand. The NS3h helicase activity is proportional to increasing lengths of the 3' un-base-paired regions up to 16 nucleotides of the RNA substrates. CSFV NS3 helicase activity requires a longer 3'-end single-stranded overhang for efficient duplex unwinding and the directionality of NS3 helicase unwinding is 3' to 5' with respect to the template strand
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
RNA helicase activity
-
-
?
ATP + H2O
ADP + phosphate
-
ATPase activity, ATP binding mode, the ATP binding site is housed between these two subdomains. In the ATP binding pocket, a Mg ion is coordinated in a octahedral manner by the beta- and gamma-phosphate oxygen atoms from ATP, two equatorial water molecules and oxygen atoms from residues Glu285 in motif II, and Thr200 in motif I, overview
-
-
?
ATP + H2O
ADP + phosphate
-
NS3 C-terminal domain catalyzes ATP hydrolysis in the presence of MgCl2 or MnCl2. MgCl2 is more effective than MnCl2 at inducing ATPase activity at concentrations ranging from 0.1 mM to 5 mM. ATP hydrolysis is required for the unwinding activity of DENV NS3H
-
-
?
ATP + H2O
ADP + phosphate
-
wild-type and mutant, NTPase activity analyzed, functional binding of RNA analyzed
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
NS3 C-terminal domain catalyzes ATP hydrolysis in the presence of MgCl2 or MnCl2. MgCl2 is more effective than MnCl2 at inducing ATPase activity at concentrations ranging from 0.1 mM to 5 mM. ATP hydrolysis is required for the unwinding activity of DENV NS3H
-
-
?
ATP + H2O
ADP + phosphate
-
wild-type and mutant, NTPase activity analyzed, functional binding of RNA analyzed
-
-
?
ATP + H2O
ADP + phosphate
-
NTPase activity
-
-
?
ATP + H2O
ADP + phosphate
-
RNA helicase activity
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
recombinant EhDEAD1 protein presents ATPase activity and is able to bind and unwind RNA in an ATPase-dependent manner
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
the 3' to 5' helicase activity of DbpA can use a 3' single-stranded loading site on either strand of the substrate helix
-
-
?
ATP + H2O
ADP + phosphate
the ATP hydrolysis activity of the extended and wild-type DbpA are measured by the pyruvate kinase/lactate dehydrogenase coupled assay. The peptide extension is not effecting the formation of the proper ATP pocket
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
preferred substrate for NTPase activity
-
-
?
ATP + H2O
ADP + phosphate
-
the C-terminal portion of hepatitis C virus nonstructural protein 3 (NS3) forms a three domain polypeptide that possesses the ability to travel along RNA or single-stranded DNA (ssDNA) in a 3 to 5 direction. Driven by the energy of ATP hydrolysis, this movement allows the protein to displace complementary strands of DNA or RNA
-
-
?
ATP + H2O
ADP + phosphate
-
the protein binds RNA and DNA in a sequence specific manner. ATP hydrolysis is stimulated by some nucleic acid polymers much better than it is stimulated by others. The range is quite dramatic. Poly(G) RNA does not stimulate at any measurable level, and poly(U) RNA (or DNA) stimulates best (up to 50 fold). HCV helicase unwinds a DNA duplex more efficiently than an RNA duplex. ATP binds HCV helicase between two RecA-like domains, causing a conformational change that leads to a decrease in the affinity of the protein for nucleic acids. One strand of RNA binds in a second cleft formed perpendicular to the ATP-binding cleft and its binding leads to stimulation of ATP hydrolysis. RNA and/or ATP binding likely causes rotation of domain 2 of the enzyme relative to domains 1 and 3, and somehow this conformational change allows the protein to move like a motor
-
-
?
ATP + H2O
ADP + phosphate
unwinds RNA in a discontinuous manner, pausing after long apparent steps of unwinding. It is proposed that the large kinetic step size of NS3 unwinding reflects a delayed, periodic release of the separated RNA product strand from a secondary binding site that is located in the NTPase domain (domain II) of NS3
-
-
?
ATP + H2O
ADP + phosphate
-
multifunctional enzyme possessing serine protease, NTPase, and RNA unwinding activities
-
-
?
ATP + H2O
ADP + phosphate
-
NTPase activity analyzed, ambiguous helicase activity, enzyme capable for unwinding RNA and DNA
-
-
?
ATP + H2O
ADP + phosphate
RNA-stimulated ATPase activities determined, interaction between the replicative component nonstructural protein 3 (NS3) with the nonstructural protein 4A (NS4A)
-
-
?
ATP + H2O
ADP + phosphate
the Arg-rich amino acid motif HCV1487-1500, a fragment of domain 2 NS3 of Hepatitis C virus, as well as the complete domain 2, and domain 2 lacking the flexible loop localized between Val1458 and Thr1476, mediate competitive inhibition of diverse protein kinase C functions, inhibition of rat brain PKC, overview
-
-
?
ATP + H2O
ADP + phosphate
-
peptide inhibitors derived from amino acid sequence of motif VI analyzed, binding of the inhibitory peptides does not interfere with the NTPase activity
-
-
?
ATP + H2O
ADP + phosphate
-
unwinding of dsRNA
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
gonadotropin-regulated testicular helicase (GRTH/DDX25), a target of gonadotropin and androgen action, is a post-transcriptional regulator of key spermatogenesis genes. GRTH has a negative role on its mRNA stability
-
-
?
ATP + H2O
ADP + phosphate
-
RHA is a coactivator in STAT6-mediated transcription, and this function is dependent on its helicase activity
-
-
?
ATP + H2O
ADP + phosphate
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation
-
-
?
ATP + H2O
ADP + phosphate
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation. DDX17 is involved in mRNA splicing
-
-
?
ATP + H2O
ADP + phosphate
-
RNA helicase A utilizes all hydrolyzable NTPs without preference. RNA helicase A unwinds dsRNA only in a 3' to 5' direction. The enzyme can only translocate on RNA possessing 3 single-stranded regions
-
-
?
ATP + H2O
ADP + phosphate
RNA-dependent ATPase, helicase activity
-
-
?
ATP + H2O
ADP + phosphate
-
the enzyme displaces partial duplex RNA exclusively in a 5' to 3' direction. This reaction is supported by ATP and dATP at relatively high concentrations. The enzyme displays only ATPase and dATPase activity. RNA helicase catalyzes the unwinding of duplex RNA and RNA*DNA hybrids provided that single-stranded RNA is available for the helicase to bind
-
-
?
ATP + H2O
ADP + phosphate
enzyme ChlR1 fails to unwind the triplex substrate in the absence of ATP or in the presence of ADP or ATPgammaS
-
-
?
ATP + H2O
ADP + phosphate
importance of the beta-phosphate for nucleotide binding
-
-
?
ATP + H2O
ADP + phosphate
the enzyme has both RNA and DNA duplex-unwinding activities with 5'-to-3' polarity
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
translation of HIV-1 gag mRNA is reliant on the ATP-dependent helicase activity of RNA helicase A
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
genome structure, crystals and three-dimensional structure determined, structure of NTP-binding region, conserved residues within the NTP-binding pocket, ATPase and RNA helicase activities determined
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation
-
-
?
ATP + H2O
ADP + phosphate
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation. DDX17 is involved in mRNA splicing
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
eIF4A may interact directly with double-stranded RNA, and recognition of helicase substrates occurs via chemical and/or structural features of the duplex. The initial rate and amplitude of duplex unwinding by eIF4A is dependent on the overall stability, rather than the length or sequence, of the duplex substrate. eIF4A helicase activity is minimally dependent on the length of the single-stranded region adjacent to the double-stranded region of the substrate. Interestingly, eIF4A is able to unwind blunt-ended duplexes. eIF4A helicase activity is also affected by substitution of 2'-OH (RNA) groups with 2'-H (DNA) or 2'-methoxyethyl groups
-
-
?
ATP + H2O
ADP + phosphate
-
the N-terminal part of the TGBp1 NTPase/helicase domain comprising conserved motifs I, Ia and II is sufficient for ATP hydrolysis, RNA binding and homologous proteinprotein interactions
-
-
?
ATP + H2O
ADP + phosphate
-
the N-terminal part of the TGBp1 NTPase/helicase domain comprising conserved motifs I, Ia and II is sufficient for ATP hydrolysis, RNA binding and homologous proteinprotein interactions
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
the ability of RNA helicases to modulate the structure and thus availability of critical RNA molecules for processing leading to protein expression is the likely mechanism by which RNA helicases contribute to differentiation. DDX17 is involved in mRNA splicing
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
Mtr4p can unwind duplex RNA in the presence of ATP and a single-stranded RNA tail in the 3' to 5' direction
-
-
?
ATP + H2O
ADP + phosphate
the DEAD-box protein DED1 has the ability to balance RNA unwinding with a profound strand annealing activity in a highly dynamic fashion
-
-
?
ATP + H2O
ADP + phosphate
ATP and dATP are the preferred nucleotide substrates. In the presence of ATP or dATP Mtr4p unwinds the duplex region of a partial duplex RNA substrate in the 3' to 5' direction. Mtr4p displays a marked preference for binding to poly(A) RNA relative to an oligoribonucleotide of the same length and a random sequence
-
-
?
ATP + H2O
ADP + phosphate
promotes RNA unwinding. The enzyme also catalyzes strand annealing. The balance between unwinding and annealing activities of DED1 depends on the RNA substrate. ADP also modulates the balance between RNA unwinding and strand annealing
-
-
?
ATP + H2O
ADP + phosphate
the Q motif regulates ATP binding and hydrolysis, the affinity of the protein for RNA substrates and the helicase activity. At least three different protein conformations that are associated with free, ADP-bound and ATP-bound forms of the protein
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
Thermochaetoides thermophila
-
-
-
?
ATP + H2O
ADP + phosphate
Thermochaetoides thermophila
-
-
-
?
ATP + H2O
ADP + phosphate
Thermochaetoides thermophila CBS 144.50
-
-
-
?
ATP + H2O
ADP + phosphate
Thermochaetoides thermophila CBS 144.50
-
-
-
?
ATP + H2O
ADP + phosphate
Thermochaetoides thermophila DSM 1495
-
-
-
?
ATP + H2O
ADP + phosphate
Thermochaetoides thermophila DSM 1495
-
-
-
?
ATP + H2O
ADP + phosphate
Thermochaetoides thermophila IMI 039719
-
-
-
?
ATP + H2O
ADP + phosphate
Thermochaetoides thermophila IMI 039719
-
-
-
?
ATP + H2O
ADP + phosphate
-
unwinding activity specific for single-strand paired RNA, does not unwind dsRNAs
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
phosphohydrolase and helicase activities of NPH-II are essential for virus replication
-
-
?
ATP + H2O
ADP + phosphate
-
unwinds duplex RNA exclusively in a 3' to 5' direction with respect to the strand to which the enzyme is bound and along which it is presumed to translocate. NTP hydrolysis by RNA bound NPH-II1 drives processive translocation of the protein in a 3 to 5 direction along the RNA strand
-
-
?
ATP + H2O
ADP + phosphate
either ATP or dATP is required for the unwinding activity, VrRH1 catalyzes unwinding of a double-stranded RNA
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
recombinant protein of C-terminal portion of NS3 protein, ATPase catalytic properties but no RNA helicase activities
-
-
?
ATP + H2O
ADP + phosphate
-
the West Nile virus RNA helicase uses the energy derived from the hydrolysis of nucleotides to separate complementary strands of RNA
-
-
?
ATP + H2O
ADP + phosphate
-
the amino acids Arg185, Arg202 and Asn417 are critical for phosphohydrolysis
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
recombinant protein of C-terminal portion of NS3 protein, ATPase catalytic properties but no RNA helicase activities
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
-
?
CTP + H2O
CDP + phosphate
helicase activity is about 85% of the activity with ATP
-
-
?
CTP + H2O
CDP + phosphate
-
NTPase activity
-
-
?
CTP + H2O
CDP + phosphate
-
-
-
?
dATP + H2O
dADP + phosphate
EF409381
either ATP or dATP is required for the unwinding activity
-
-
?
dATP + H2O
dADP + phosphate
helicase activity is about 10% of the activity with ATP
-
-
?
dATP + H2O
dADP + phosphate
-
the enzyme displaces partial duplex RNA exclusively in a 5' to 3' direction. This reaction is supported by ATP and dATP at relatively high concentrations. The enzyme displays only ATPase and dATPase activity. RNA helicase catalyzes the unwinding of duplex RNA and RNA*DNA hybrids provided that single-stranded RNA is available for the helicase to bind
-
-
?
dATP + H2O
dADP + phosphate
ATP and dATP are the preferred nucleotide substrates. In the presence of ATP or dATP Mtr4p unwinds the duplex region of a partial duplex RNA substrate in the 3' to 5' direction. Mtr4p displays a marked preference for binding to poly(A) RNA relative to an oligoribonucleotide of the same length and a random sequence
-
-
?
dATP + H2O
dADP + phosphate
either ATP or dATP is required for the unwinding activity, VrRH1 catalyzes unwinding of a double-stranded RNA
-
-
?
GTP + H2O
GDP + phosphate
helicase activity is about 55% of the activity with ATP
-
-
?
GTP + H2O
GDP + phosphate
-
NTPase activity
-
-
?
GTP + H2O
GDP + phosphate
-
-
-
?
GTP + H2O
GDP + phosphate
-
49% of the phosphohydrolase activity with ATP
-
-
?
RNA + H2O
?
-
RNA unwinding activity, the enzyme contains two RecA-like domains, opening and closing of the interdomain cleft during RNA unwinding
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-
?
RNA + H2O
?
-
RNA unwinding activity, substrate is a 154mer of 23S rRNA generated by T7 polymerase from in vitro transcription
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-
?
RNA + H2O
?
EF409381
helicase/unwinding activity, either ATP or dATP is required for the unwinding activity
-
-
?
RNA + H2O
?
NS3 helicase domain helicase activity is dependent on the presence of NTP and divalent cations, with a preference for ATP and Mn2+, and requires a substrates possessing a 3' un-base-paired region on the RNA template strand. The helicase activity is proportional to increasing lengths of the 3' un-base-paired regions up to 16 nucleotides of theRNA substrates, overview
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-
?
RNA + H2O
?
NS3 helicase domain helicase activity is dependent on the presence of NTP and divalent cations, with a preference for ATP and Mn2+, and requires a substrates possessing a 3' un-base-paired region on the RNA template strand. The helicase activity is proportional to increasing lengths of the 3' un-base-paired regions up to 16 nucleotides of theRNA substrates, overview
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-
?
RNA + H2O
?
-
helicase/unwinding activity, ATP hydrolysis is required for the unwinding activity of DENV NS3H
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-
?
RNA + H2O
?
-
RNA helicase actiivty
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-
?
RNA + H2O
?
-
helicase/unwinding activity
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-
?
RNA + H2O
?
unwinding helicase activity, NS3 is ahighly basic protein with multiple RNA binding sites
-
-
?
UTP + H2O
UDP + phosphate
helicase activity is about 55% of the activity with ATP
-
-
?
UTP + H2O
UDP + phosphate
-
NTPase activity
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-
?
UTP + H2O
UDP + phosphate
-
-
-
?
additional information
?
-
-
using yeast two-hybrid and pull-down assays it is shown that RH22 interacts with the 50S ribosomal protein RPL24
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-
?
additional information
?
-
ISE2 associates with numerous chloroplast RNA species, chloroplast rRNAs are potential ISE2 substrates. ISE2 associates with transcripts containing C-to-U editing sites
-
-
-
additional information
?
-
-
ISE2 associates with numerous chloroplast RNA species, chloroplast rRNAs are potential ISE2 substrates. ISE2 associates with transcripts containing C-to-U editing sites
-
-
-
additional information
?
-
ISE2 associates with numerous chloroplast RNA species, chloroplast rRNAs are potential ISE2 substrates. ISE2 associates with transcripts containing C-to-U editing sites
-
-
-
additional information
?
-
-
open helicase conformation in the absence of nucleotides, or in the presence of ATP, or ADP, or RNA. In the presence of ADP and RNA, the open conformation is retained. By contrast, cooperative binding of ATP and RNA leads to a compact helicase structure, direct transitions between open and closed conformations, overview
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-
?
additional information
?
-
-
BMV 1a protein accumulates on endoplasmic reticulum membranes of the host cell, recruits the other RNA replication factor 2apol and induces 50- to 70-nm membrane invaginations serving as RNA replication compartments, BMV 1a protein also recruits viral replication templates such as genomic RNA3 depending on the BMV 1a protein helicase motif, in absence of 2apol, BMV 1a protein highly stabilizes RNA3 by transferring it to a membrane-associated, nuclease-resistant state, overview
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-
?
additional information
?
-
-
multifunctional enzyme showing protease, helicase, and NTPase activities, the enzyme has a function in RNA replication complex assembly besides its function in RNA synthesis/capping, the enzyme activity is located in the C-terminal nucleoside triphosphatase/helicase domain of the BMV 1a protein RNA replication factor
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-
?
additional information
?
-
-
DEAD box proteins are putative RNA unwinding proteins, BmL3-helicase also is a DEAD box RNA helicase
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-
?
additional information
?
-
EF409381
DEAD box proteins are putative RNA unwinding proteins, BmL3-helicase also is a DEAD box RNA helicase
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-
?
additional information
?
-
-
nonstructural protein 3 (NS3) possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus
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-
?
additional information
?
-
nonstructural protein 3 (NS3) possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus
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-
?
additional information
?
-
-
NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules
-
-
?
additional information
?
-
NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules
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-
?
additional information
?
-
NS3 possesses three enzyme activities that are likely to be essential for virus replication: a serine protease located in the N-terminus and NTPase as well as helicase activities located in the C-terminus. Functions of NS3 and NS5B during positive-strand RNA virus replication, the NS3 protein is be involved in the unwinding of the viral RNA template while NS5B protein may be involved in catalyzing the synthesis of new RNA molecules
-
-
?
additional information
?
-
-
the enzyme plays an important role in viral replication
-
-
?
additional information
?
-
-
multifunctional enzyme showing protease, helicase, and NTPase activities
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-
?
additional information
?
-
-
The NS3 protein physically associates with the NS5 polymerase, NS3 andNS5 carry out all the enzymatic activities needed for polyprotein processing and genome replication. NS3 possesses an ATPase/helicase and RNA triphosphatase at its C-terminal end that are essential for RNA replication. In addition to its known enzymatic functions, the NS3 protein appears to be involved in the assembly of an infectious flaviviral particle, through its interactions with NS2A and presumably host cell proteins
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-
?
additional information
?
-
-
conformational changes during ATP hydrolysis and RNA unwinding: on ssRNA binding, the NS3 enzyme switches to a catalytic competent state imparted by an inward movement of the P-loop, interdomain closure and a change in the divalent metal coordination shell, providing a structural basis for RNA-stimulated ATP hydrolysis. Determination of enzyme structure-function relationship of enzyme bound to single-stranded RNA, to an ATP analogue, to a transition-state analogue and to ATP hydrolysis products. RNA recognition appears largely sequence independent, reaction mechanism and RNA recognition, overview. RNA-unwinding mechanism, overview
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-
?
additional information
?
-
-
the C-terminal region of NS3 forms the RNA helicase domain, an ATP-driven molecular motor
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-
?
additional information
?
-
-
the helicase domain of Dengue virus NS3 protein, i.e. DENV NS3H, contains RNA-stimulated nucleoside triphosphatase, NTPase, ATPase/helicase, and RNA 5'-triphosphatase, RTPase, activities that are essential for viral RNA replication and capping. A 5'-tailed RNA is a better RTPase substrate than an RNA containing no 5'-dangling nucleotide
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-
?
additional information
?
-
-
RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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-
?
additional information
?
-
-
the helicase domain of Dengue virus NS3 protein, i.e. DENV NS3H, contains RNA-stimulated nucleoside triphosphatase, NTPase, ATPase/helicase, and RNA 5'-triphosphatase, RTPase, activities that are essential for viral RNA replication and capping. A 5'-tailed RNA is a better RTPase substrate than an RNA containing no 5'-dangling nucleotide
-
-
?
additional information
?
-
-
nonstructural proteins NS3 and NS5 form complexes in infected mammalian cells
-
-
?
additional information
?
-
-
substrate specificity, bifunctional enzyme, NS3 is an RNA-stimulated nucleoside triphosphatase NTPase/RNA helicase and a 5'-RNA triphosphatase RTPase, overview, the full-length NS3 with or without NS2B cofactor domain exhibits a catalytically more efficient RNA helicase activity than the N-terminally-truncated NS3 helicase domain, suggesting that the protease domain enhances RNA helicase activity
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-
?
additional information
?
-
-
helicase B, RhlB, is one of the five DEAD box RNA-dependent ATPases in Escherichia coli. ATPases found in Escherichia coli. RhlB requires an interaction with the partner protein RNase E for appreciable ATPase and RNA unwinding activities
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-
?
additional information
?
-
-
RhlB is the only Escherichia coli DEAD box protein that requires a protein partner to stimulate its ATPase activity
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-
?
additional information
?
-
analysis of ATPase and unwinding activities of CsdA_564 and CsdA_1-445, and of RNA-binding properties of the C-terminal regions of CsdA and CsdA_RNA-binding domain, overview
-
-
-
additional information
?
-
the helicase activity of wild-type DbpA and the extended DbpA is investigated by measuring the unwinding of the 5'-32P labeled 9-mer annealed to the unlabeled 32-mer RNA, 32-mer RNA-DNA or the RNA-PEG chimera. DbpA performs RNA structural isomerizations in the ribosome. The only requirement for a double-helix to serve as a DbpA substrate is for the double-helix to be positioned within the catalytic core's grasp. The RecA-like domains of the DEAD-box proteins, which form their catalytic core, attack one strand of the RNA double-helix and bend it. The bending process forces the release of the complementary RNA strand. The ATP-binding to the RecA-like domains provides the energy for the single-stranded RNA bending, while the ATP hydrolysis causes the release of the second strand of the double-helix from the catalytic core and the regeneration of the enzymes. The extension of the interdomain linker region has no effect on the ability of DbpA to perform its helicase function. Thus, the physical connection of DbpA RNA binding domain to the catalytic core is unimportant for the helicase activity of DbpA, suggesting the DbpA protein is a region-specific enzyme, which would unwind any double-helix substrate near hairpin 92
-
-
-
additional information
?
-
-
the enzyme is involved in viral replication
-
-
?
additional information
?
-
-
the multifunctional enzyme shows RNA-dependent NTPase and helicase activities, no activity with ADP and AMP
-
-
?
additional information
?
-
-
the mature NS3 protein comprises 5 domains: the N-terminal 2 domains form the serine protease along with the NS4A cofactor, and the C-terminal 3 domains form the helicase. The helicase portion of NS3 can be separated form the protease portion by cleaving a linker. Since the protease portion is more hydrophobic, removing it allows the NS3 helicase fragment to be expressed as a more soluble protein at higher levels in Escherichia coli. The fragment of NS3 possessing helicase activity is referred to as HCV helicase
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-
?
additional information
?
-
-
the C-terminal region of NS3 exhibits RNA-stimulated NTPase, e.g. ATPase, and helicase activity, while the N-terminal serine protease domain of NS3 enhances RNA binding and unwinding by the C-terminal region, NS4A mutants that are defective in ATP-coupled RNA binding are lethal in vivo
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-
?
additional information
?
-
the C-terminal region of NS3 exhibits RNA-stimulated NTPase, e.g. ATPase, and helicase activity, while the N-terminal serine protease domain of NS3 enhances RNA binding and unwinding by the C-terminal region, NS4A mutants that are defective in ATP-coupled RNA binding are lethal in vivo
-
-
?
additional information
?
-
-
RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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-
?
additional information
?
-
-
DEAD-Box RNA Helicase DDX3 interacts with DDX5. The protein-protein interaction is increased in the G2/M phase
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-
?
additional information
?
-
DEAD-Box RNA Helicase DDX3 interacts with DDX5. The protein-protein interaction is increased in the G2/M phase
-
-
?
additional information
?
-
-
human telomerase RNA interacts with the N-terminal domain of RHAU
-
-
?
additional information
?
-
p68 interacts with an intronic splicing activator, RNA binding motif protein 4 (RBM4), thereby stimulating tau exon 10 inclusion
-
-
?
additional information
?
-
-
recombinant N-terminal, central helicase, and C-terminal domains of RHA are evaluated for their ability to specifically interact with cognate RNAs by in vitro biochemical measurements and mRNA translation assays in cells. Results demonstrate that N-terminal residues confer selective interaction with retroviral and junD target RNAs. Conserved lysine residues in the distal alpha-helix of the double-stranded RNA-binding domains are necessary to engage structural features of retroviral and junD 5'-UTRs
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-
?
additional information
?
-
-
RNA helicase A interacts with La ribonucleoprotein domain family member 6 (LARP6) which recruits RHA to the 5' UTR of collagen mRNAs
-
-
?
additional information
?
-
ChlR1 robustly unwinds DNA triplex substrates in an ATP-dependent manner requiring an 5'-ssDNA tail, ChlR1 can unwind an intramolecular triplex structure
-
-
?
additional information
?
-
-
ChlR1 robustly unwinds DNA triplex substrates in an ATP-dependent manner requiring an 5'-ssDNA tail, ChlR1 can unwind an intramolecular triplex structure
-
-
?
additional information
?
-
enzyme DDX21 inhibits influenza A virus replication. Enzyme DDX21 most likely binds viral PB1 protein in the cytoplasm, where protein PB1 is probably free of the other polymerase subunits, albeit transiently, before it forms a complex with viral protein PA that is imported into the nucleus
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-
?
additional information
?
-
human Upf1 is able to translocate slowly over long single-stranded nucleic acids with a high processivity. Upf1 efficiently translocates through double-stranded structures and protein-bound sequences. The helicase domain of Upf1 is capable of both unwinding double-stranded nucleic acids and translocation on single-stranded nucleic acids over long distances. Upf1 remodels nucleoprotein complexes
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-
?
additional information
?
-
-
human Upf1 is able to translocate slowly over long single-stranded nucleic acids with a high processivity. Upf1 efficiently translocates through double-stranded structures and protein-bound sequences. The helicase domain of Upf1 is capable of both unwinding double-stranded nucleic acids and translocation on single-stranded nucleic acids over long distances. Upf1 remodels nucleoprotein complexes
-
-
?
additional information
?
-
RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
-
-
?
additional information
?
-
RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
-
-
?
additional information
?
-
wild-type and mutant enzymes in vitro RNA binding and unwinding or in the cell during HIV-1 production during RNA helicase A-RNA interaction and RNA helicase A-stimulated viral RNA processes, overview
-
-
?
additional information
?
-
RNA-dependent interactions of DHX34 with UPF3b and the EJC component, MLN51, no interaction with PABP1, with the eukaryotic release factor eRF3, or with the NMD core factor UPF2. Interactions of DHX34 with RNA degradation factors such as the exonuclease XRN1, the exosome component DIS3, and the decapping enzyme DCP1, all of them independently of the presence of RNA. DHX34 interacts with UPF1 directly and preferentially associates with SURF complexes, and promoties UPF1 phosphorylation
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-
?
additional information
?
-
-
RNA-dependent interactions of DHX34 with UPF3b and the EJC component, MLN51, no interaction with PABP1, with the eukaryotic release factor eRF3, or with the NMD core factor UPF2. Interactions of DHX34 with RNA degradation factors such as the exonuclease XRN1, the exosome component DIS3, and the decapping enzyme DCP1, all of them independently of the presence of RNA. DHX34 interacts with UPF1 directly and preferentially associates with SURF complexes, and promoties UPF1 phosphorylation
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-
?
additional information
?
-
the enzyme DDX21 binds to the RNA binding domain of viral NS1 protein, specifically to a region comprised of amino acids R37, R38, K41 and R44
-
-
?
additional information
?
-
the purified recombinant ChlR1 protein is a DNA-dependent ATPase and unwinds partial duplex DNA substrates with a preferred 5' to 3' directionality, triplex DNA is the preferred DNA substrate for ChlR1, analysis of diverse DNA substrates, overview
-
-
?
additional information
?
-
-
the purified recombinant ChlR1 protein is a DNA-dependent ATPase and unwinds partial duplex DNA substrates with a preferred 5' to 3' directionality, triplex DNA is the preferred DNA substrate for ChlR1, analysis of diverse DNA substrates, overview
-
-
?
additional information
?
-
Upf1-HD is a slow translocase compared with other monomeric helicases like UvrD and NS3, but is able to translocate slowly over long single-stranded nucleic acids with a high processivity which exceeds the size of the tested hairpins, overview. Enzyme Upf1 is able to both unwind a long dsRNA of 156 bp and translocate onto ssRNA. Active translocating enzyme Upf1 disrupts protein-nucleic acid interactions. Upf1 remodels nucleoprotein complexes. Substrates are RNADNA hybrids, ssDNA and ssRNA
-
-
?
additional information
?
-
-
Upf1-HD is a slow translocase compared with other monomeric helicases like UvrD and NS3, but is able to translocate slowly over long single-stranded nucleic acids with a high processivity which exceeds the size of the tested hairpins, overview. Enzyme Upf1 is able to both unwind a long dsRNA of 156 bp and translocate onto ssRNA. Active translocating enzyme Upf1 disrupts protein-nucleic acid interactions. Upf1 remodels nucleoprotein complexes. Substrates are RNADNA hybrids, ssDNA and ssRNA
-
-
?
additional information
?
-
wild-type and mutant enzymes in vitro RNA binding and unwinding or in the cell during HIV-1 production during RNA helicase A-RNA interaction and RNA helicase A-stimulated viral RNA processes, overview. Ability of wild-type and mutant RHAs to stimulate the accumulation of HIV-1 mRNAs
-
-
?
additional information
?
-
enzyme Brr2 catalyzes an ATP-dependent unwinding of the U4/U6 RNA duplex
-
-
-
additional information
?
-
multiple cross-links between Aquarius and hSyf1, hIsy1, CCDC16 or CypE, with the majority of the cross-linked residues located in domains or structural insertions specific for Aquarius, such as the ARM, pointer and thumb domains, and in the large insertions of the beta-barrel
-
-
-
additional information
?
-
-
multiple cross-links between Aquarius and hSyf1, hIsy1, CCDC16 or CypE, with the majority of the cross-linked residues located in domains or structural insertions specific for Aquarius, such as the ARM, pointer and thumb domains, and in the large insertions of the beta-barrel
-
-
-
additional information
?
-
Aquarius exhibits ATPase and RNA-unwinding activity in vitro. Consistently with its possessing a Q motif and thus specifically binding ATP, Aquarius does not hydrolyze GT. Aquarius does not bind a blunt-ended RNA duplex
-
-
-
additional information
?
-
-
Aquarius exhibits ATPase and RNA-unwinding activity in vitro. Consistently with its possessing a Q motif and thus specifically binding ATP, Aquarius does not hydrolyze GT. Aquarius does not bind a blunt-ended RNA duplex
-
-
-
additional information
?
-
Brr2 participates in a transient opening of the catalytic core between the 2 steps of splicing, which is characterized by the intermittent disruption of U6-5SS and U2-U6 interactions
-
-
-
additional information
?
-
-
Brr2 participates in a transient opening of the catalytic core between the 2 steps of splicing, which is characterized by the intermittent disruption of U6-5SS and U2-U6 interactions
-
-
-
additional information
?
-
DHX8 has an in vitro binding preference for adenine-rich RNA, and RNA binding triggers the release of ADP through significant conformational flexibility in the conserved DEAH-, P-loop and hook-turn motifs. DHX8 makes base-specific contacts with RNA and preferentially binds adenine-rich RNA in vitro, RNA-bound DHX8DELTA547-A6 structure, overview. RNA binding triggers nucleotide release and establish the importance of R620 and both the hook-loop and hook-turn for DHX8 helicase activity, proposing that the hook-turn acts as a gatekeeper to aid correct directional RNA movement through the RNA-binding tunnel. Unwinding activity using an RNA/DNA duplex substrate comprising a 60-mer RNA strand (RNA60) annealed to a 30-mer DNA strand fluorescently labelled on the 30 end (DNA30-ATTO680). DHX8 is an RNA-specific helicase by showing that a poly(dA)10 DNA strand cannot displace Cy5-poly(A)10 from DHX8 in the presence of ADP-AlFx. The displacement of the probe with poly(A)10, poly(C)10, poly(G)10 and poly(U)10 RNA indicates that DHX8 has a preference for binding adenine-rich sequences as the rank ascending order of IC50 values is poly (A)10, poly(U)10, poly(C)10, and poly(G)10. Molecular details of RNA binding to DHX8, the RNA base stack is bookended by the beta-hairpin and the hook-turn hairpin, DHX8 forms RNA base-specific interactions through its OB-fold and RecA1 domains, overview
-
-
-
additional information
?
-
-
DHX8 has an in vitro binding preference for adenine-rich RNA, and RNA binding triggers the release of ADP through significant conformational flexibility in the conserved DEAH-, P-loop and hook-turn motifs. DHX8 makes base-specific contacts with RNA and preferentially binds adenine-rich RNA in vitro, RNA-bound DHX8DELTA547-A6 structure, overview. RNA binding triggers nucleotide release and establish the importance of R620 and both the hook-loop and hook-turn for DHX8 helicase activity, proposing that the hook-turn acts as a gatekeeper to aid correct directional RNA movement through the RNA-binding tunnel. Unwinding activity using an RNA/DNA duplex substrate comprising a 60-mer RNA strand (RNA60) annealed to a 30-mer DNA strand fluorescently labelled on the 30 end (DNA30-ATTO680). DHX8 is an RNA-specific helicase by showing that a poly(dA)10 DNA strand cannot displace Cy5-poly(A)10 from DHX8 in the presence of ADP-AlFx. The displacement of the probe with poly(A)10, poly(C)10, poly(G)10 and poly(U)10 RNA indicates that DHX8 has a preference for binding adenine-rich sequences as the rank ascending order of IC50 values is poly (A)10, poly(U)10, poly(C)10, and poly(G)10. Molecular details of RNA binding to DHX8, the RNA base stack is bookended by the beta-hairpin and the hook-turn hairpin, DHX8 forms RNA base-specific interactions through its OB-fold and RecA1 domains, overview
-
-
-
additional information
?
-
substrate determinants for unwinding activity of the DExH/D-Box protein RNA helicase A, overview. RHA translocates efficiently along the 3' overhang of RNA, but not DNA, with a requirement of covalent continuity. Ribose-phosphate backbone lesions on both strands of the nucleic acids, especially on the 3' overhang of the loading strand, affect RHA unwinding significantly. RHA requires RNA on the 3' overhang which directly or indirectly connects with the duplex region to mediate productive unwinding
-
-
-
additional information
?
-
the two isoforms of UPF differ in their RNA-binding and catalytic activities, the flexible loop in domain 1B affects the catalytic activity of UPF1 isozymes
-
-
-
additional information
?
-
RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
-
-
?
additional information
?
-
RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
-
-
?
additional information
?
-
RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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-
?
additional information
?
-
helicase DDX6 colocalizes with TRIM32 in neural stem cells and neurons and increases the activity of Let-7a. The activation of Let-7a depends on the enzyme's helicase activity
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-
?
additional information
?
-
-
RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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-
?
additional information
?
-
interactions of FRH with RNA and ADP, overview
-
-
-
additional information
?
-
-
interactions of FRH with RNA and ADP, overview
-
-
-
additional information
?
-
interactions of FRH with RNA and ADP, overview
-
-
-
additional information
?
-
interactions of FRH with RNA and ADP, overview
-
-
-
additional information
?
-
interactions of FRH with RNA and ADP, overview
-
-
-
additional information
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interactions of FRH with RNA and ADP, overview
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additional information
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interactions of FRH with RNA and ADP, overview
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additional information
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the NS3 protein of Rice hoja blanca virus is an RNA silencing suppressor, RSS, that exclusively binds to small dsRNA molecules. This plant viral RSS lacks interferon antagonistic activity, yet it is able to substitute the RSS function of the Tat protein of Human immunodeficiency virus type 1 based on the sequestration of small dsRNA. NS3 is able to inhibit endogenous miRNA action in mammalian cells
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additional information
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the NS3 protein of Rice hoja blanca virus is an RNA silencing suppressor, RSS, that exclusively binds to small dsRNA molecules. This plant viral RSS lacks interferon antagonistic activity, yet it is able to substitute the RSS function of the Tat protein of Human immunodeficiency virus type 1 based on the sequestration of small dsRNA. NS3 is able to inhibit endogenous miRNA action in mammalian cells
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additional information
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the NS3 protein of Rice hoja blanca virus is an RNA silencing suppressor, RSS, that exclusively binds to small dsRNA molecules. This plant viral RSS lacks interferon antagonistic activity, yet it is able to substitute the RSS function of the Tat protein of Human immunodeficiency virus type 1 based on the sequestration of small dsRNA. NS3 is able to inhibit endogenous miRNA action in mammalian cells
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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additional information
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Brr2 participates in a transient opening of the catalytic core between the 2 steps of splicing, which is characterized by the intermittent disruption of U6-5SS and U2-U6 interactions
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additional information
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Brr2 participates in a transient opening of the catalytic core between the 2 steps of splicing, which is characterized by the intermittent disruption of U6-5SS and U2-U6 interactions
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additional information
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Brr2 participates in a transient opening of the catalytic core between the 2 steps of splicing, which is characterized by the intermittent disruption of U6-5SS and U2-U6 interactions
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additional information
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purified CshA exhibits typical RNA helicase activities, as exemplified by RNA-dependent ATPase activity and unwinding of the DNA-RNA duplex. Unlabeled duplex DNA oligonucleotide is used as helicase substrate, molecular dynamics, overview
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additional information
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purified CshA exhibits typical RNA helicase activities, as exemplified by RNA-dependent ATPase activity and unwinding of the DNA-RNA duplex. Unlabeled duplex DNA oligonucleotide is used as helicase substrate, molecular dynamics, overview
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additional information
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purified CshA exhibits typical RNA helicase activities, as exemplified by RNA-dependent ATPase activity and unwinding of the DNA-RNA duplex. Unlabeled duplex DNA oligonucleotide is used as helicase substrate, molecular dynamics, overview
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additional information
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purified CshA exhibits typical RNA helicase activities, as exemplified by RNA-dependent ATPase activity and unwinding of the DNA-RNA duplex. Unlabeled duplex DNA oligonucleotide is used as helicase substrate, molecular dynamics, overview. Recombinant N-terminal His-tagged CshA (gene SA1885, N315 genome) binds to 375-nt sarA mRNA
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additional information
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purified CshA exhibits typical RNA helicase activities, as exemplified by RNA-dependent ATPase activity and unwinding of the DNA-RNA duplex. Unlabeled duplex DNA oligonucleotide is used as helicase substrate, molecular dynamics, overview. Recombinant N-terminal His-tagged CshA (gene SA1885, N315 genome) binds to 375-nt sarA mRNA
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additional information
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purified CshA exhibits typical RNA helicase activities, as exemplified by RNA-dependent ATPase activity and unwinding of the DNA-RNA duplex. Unlabeled duplex DNA oligonucleotide is used as helicase substrate, molecular dynamics, overview. Recombinant N-terminal His-tagged CshA (gene SA1885, N315 genome) binds to 375-nt sarA mRNA
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additional information
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purified CshA exhibits typical RNA helicase activities, as exemplified by RNA-dependent ATPase activity and unwinding of the DNA-RNA duplex. Unlabeled duplex DNA oligonucleotide is used as helicase substrate, molecular dynamics, overview. Recombinant N-terminal His-tagged CshA (gene SA1885, N315 genome) binds to 375-nt sarA mRNA
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additional information
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purified CshA exhibits typical RNA helicase activities, as exemplified by RNA-dependent ATPase activity and unwinding of the DNA-RNA duplex. Unlabeled duplex DNA oligonucleotide is used as helicase substrate, molecular dynamics, overview
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additional information
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Thermochaetoides thermophila
RNA loading mechanism of Prp43, and catalytic mechanism, detailed overview. Prp43 binds RNA in a sequence-independent fashion. Analysis of interactions between Prp43 and the U7-RNA and of the ATP-bound enzyme structure. Prp43 adopts an open conformation after ATP binding and switches into the closed conformation after binding to RNA. Prp43 translocates RNA via its Hook-Turn
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additional information
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Thermochaetoides thermophila CBS 144.50
RNA loading mechanism of Prp43, and catalytic mechanism, detailed overview. Prp43 binds RNA in a sequence-independent fashion. Analysis of interactions between Prp43 and the U7-RNA and of the ATP-bound enzyme structure. Prp43 adopts an open conformation after ATP binding and switches into the closed conformation after binding to RNA. Prp43 translocates RNA via its Hook-Turn
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additional information
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Thermochaetoides thermophila DSM 1495
RNA loading mechanism of Prp43, and catalytic mechanism, detailed overview. Prp43 binds RNA in a sequence-independent fashion. Analysis of interactions between Prp43 and the U7-RNA and of the ATP-bound enzyme structure. Prp43 adopts an open conformation after ATP binding and switches into the closed conformation after binding to RNA. Prp43 translocates RNA via its Hook-Turn
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additional information
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Thermochaetoides thermophila IMI 039719
RNA loading mechanism of Prp43, and catalytic mechanism, detailed overview. Prp43 binds RNA in a sequence-independent fashion. Analysis of interactions between Prp43 and the U7-RNA and of the ATP-bound enzyme structure. Prp43 adopts an open conformation after ATP binding and switches into the closed conformation after binding to RNA. Prp43 translocates RNA via its Hook-Turn
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additional information
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TaRH1-catalysed unwinding of duplex RNA
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additional information
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ATP-dependent unwinding of duplex RNA in vitro by TaRH1
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additional information
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the enzyme is unable to unwind duplex DNA
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additional information
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NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain presumably involved in viral replication
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additional information
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NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain
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additional information
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NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain presumably involved in viral replication
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additional information
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NS3 possess both protease and helicase activities, the C-terminal portion of the NS3 contains the ATPase/helicase domain
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additional information
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NS3 includes a protease and a helicase that are essential to virus replication and to RNA capping
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additional information
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NS3 includes a protease and a helicase that are essential to virus replication and to RNA capping
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additional information
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RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. Upon enzyme loading, the RNA helicase is able to locally open the RNA duplex facilitating the formation of a single-stranded structure. The proposed model for the catalytic activity of this group of RNA helicases suggests that the hydrolysis of ATP occurs before the strand separation. ATP hydrolysis is essential for the efficient release of the free enzyme from the RNA. The process is performed locally without any displacement of the enzyme along the RNA strands. Some proteins harboring helicase domains are able to recognize specific patterns in RNA molecules, bind to them and act as a skeleton to build ribonucleoprotein complexes without a specific catalytic activity over the RNA secondary structures
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evolution
ChlR1 is a superfamily 2 DNA helicase that contains a conserved iron-sulfur domain. In humans exist four iron-sulfur DNA helicases, XPD, FANCJ, RTEL1, and ChlR1, that are implicated in autosomal recessive genetic diseases
evolution
enzyme DHX34 belongs to the DExH/D box family of proteins
evolution
RNA helicase A (RHA) is a DExH-box RNA helicase
evolution
RNA helicases are a large family of enzymes including evolutionarily conserved Hel-1
evolution
the putative ATP-dependent RNA helicase and is a member of the DEAD-box family of SF2, superfamily 2, phylogenetic tree and analysis
evolution
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the RNA helicase ubiquitous group of proteins is found in all the kingdoms of life, ranging from viruses to mammals, and it is closely related to DNA helicases. RNA helicases are included in five of the six nucleic acid helicase superfamilies. RNA helicases belonging to superfamilies SF3, SF4, and SF5 are oligomeric proteins (mostly hexamers), being typically encoded by genomes of viruses or bacteria. Superfamilies SF1 and SF2 of RNA helicases are non-oligomeric proteins, containing a conserved bi-lobular core composed by two RecA-like domains as a central structure. Several sub-families of RNA helicases are also defined on the basis of their sequence conservation and biological activity. Human RNA helicases are included in five different sub-families: Upf1-like, DEAD-box, DEAH-RHA, RIG-I like and Ski2-like proteins. The Upf1-like sub-family belongs to the SF1 superfamily, and includes a group of enzymes involved in RNA metabolism centered in processes like splicing or nonsense-mediated decay. The SF2 superfamily includes five different sub-families of RNA helicases: DEAD-box helicases, DEAH-RHA helicases, RIG-I like proteins, Ski2-like proteins and the NS3/NPH-II subfamily. SF1 and SF2 RNA helicases have other variable accessory domains located around their structural cores which frequently contain specific additional functionalities such as DNA-binding, protein-binding or oligomerization. Structure-function relationships of the most widely-studied families of RNA helicases: the DEAD-box, RIG-I-like and viral NS3 classes, overview. Enzyme NS3 falls within NS3/NPH-II subfamily of SF2 helicase superfamily
evolution
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the RNA helicase ubiquitous group of proteins is found in all the kingdoms of life, ranging from viruses to mammals, and it is closely related to DNA helicases. RNA helicases are included in five of the six nucleic acid helicase superfamilies. RNA helicases belonging to superfamilies SF3, SF4, and SF5 are oligomeric proteins (mostly hexamers), being typically encoded by genomes of viruses or bacteria. Superfamilies SF1 and SF2 of RNA helicases are non-oligomeric proteins, containing a conserved bi-lobular core composed by two RecA-like domains as a central structure. Several sub-families of RNA helicases are also defined on the basis of their sequence conservation and biological activity. Human RNA helicases are included in five different sub-families: Upf1-like, DEAD-box, DEAH-RHA, RIG-I like and Ski2-like proteins. The Upf1-like sub-family belongs to the SF1 superfamily, and includes a group of enzymes involved in RNA metabolism centered in processes like splicing or nonsense-mediated decay. The SF2 superfamily includes five different sub-families of RNA helicases: DEAD-box helicases, DEAH-RHA helicases, RIG-I like proteins, Ski2-like proteins and the NS3/NPH-II subfamily. SF1 and SF2 RNA helicases have other variable accessory domains located around their structural cores which frequently contain specific additional functionalities such as DNA-binding, protein-binding or oligomerization. Structure-function relationships of the most widely-studied families of RNA helicases: the DEAD-box, RIG-I-like and viral NS3 classes, overview. Enzyme NS3 falls within NS3/NPH-II subfamily of SF2 helicase superfamily
evolution
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the RNA helicase ubiquitous group of proteins is found in all the kingdoms of life, ranging from viruses to mammals, and it is closely related to DNA helicases. RNA helicases are included in five of the six nucleic acid helicase superfamilies. RNA helicases belonging to superfamilies SF3, SF4, and SF5 are oligomeric proteins (mostly hexamers), being typically encoded by genomes of viruses or bacteria. Superfamilies SF1 and SF2 of RNA helicases are non-oligomeric proteins, containing a conserved bi-lobular core composed by two RecA-like domains as a central structure. Several sub-families of RNA helicases are also defined on the basis of their sequence conservation and biological activity. Human RNA helicases are included in five different sub-families: Upf1-like, DEAD-box, DEAH-RHA, RIG-I like and Ski2-like proteins. The Upf1-like sub-family belongs to the SF1 superfamily, and includes a group of enzymes involved in RNA metabolism centered in processes like splicing or nonsense-mediated decay. The SF2 superfamily includes five different sub-families of RNA helicases: DEAD-box helicases, DEAH-RHA helicases, RIG-I like proteins, Ski2-like proteins and the NS3/NPH-II subfamily. SF1 and SF2 RNA helicases have other variable accessory domains located around their structural cores which frequently contain specific additional functionalities such as DNA-binding, protein-binding or oligomerization. Structure-function relationships of the most widely-studied families of RNA helicases: the DEAD-box, RIG-I-like and viral NS3 classes, overview. Enzyme NS3 falls within NS3/NPH-II subfamily of SF2 helicase superfamily
evolution
the RNA helicase ubiquitous group of proteins is found in all the kingdoms of life, ranging from viruses to mammals, and it is closely related to DNA helicases. RNA helicases are included in five of the six nucleic acid helicase superfamilies. RNA helicases belonging to superfamilies SF3, SF4, and SF5 are oligomeric proteins (mostly hexamers), being typically encoded by genomes of viruses or bacteria. Superfamilies SF1 and SF2 of RNA helicases are non-oligomeric proteins, containing a conserved bi-lobular core composed by two RecA-like domains as a central structure. Several sub-families of RNA helicases are also defined on the basis of their sequence conservation and biological activity. Human RNA helicases are included in five different sub-families: Upf1-like, DEAD-box, DEAH-RHA, RIG-I like and Ski2-like proteins. The Upf1-like sub-family belongs to the SF1 superfamily, and includes a group of enzymes involved in RNA metabolism centered in processes like splicing or nonsense-mediated decay. The SF2 superfamily includes five different sub-families of RNA helicases: DEAD-box helicases, DEAH-RHA helicases, RIG-I like proteins, Ski2-like proteins and the NS3/NPH-II subfamily. SF1 and SF2 RNA helicases have other variable accessory domains located around their structural cores which frequently contain specific additional functionalities such as DNA-binding, protein-binding or oligomerization. Structure-function relationships of the most widely-studied families of RNA helicases: the DEAD-box, RIG-I-like and viral NS3 classes, overview. Enzyme NS3 falls within NS3/NPH-II subfamily of SF2 helicase superfamily
evolution
the RNA helicase ubiquitous group of proteins is found in all the kingdoms of life, ranging from viruses to mammals, and it is closely related to DNA helicases. RNA helicases are included in five of the six nucleic acid helicase superfamilies. RNA helicases belonging to superfamilies SF3, SF4, and SF5 are oligomeric proteins (mostly hexamers), being typically encoded by genomes of viruses or bacteria. Superfamilies SF1 and SF2 of RNA helicases are non-oligomeric proteins, containing a conserved bi-lobular core composed by two RecA-like domains as a central structure. Several sub-families of RNA helicases are also defined on the basis of their sequence conservation and biological activity. Human RNA helicases are included in five different sub-families: Upf1-like, DEAD-box, DEAH-RHA, RIG-I like and Ski2-like proteins. The Upf1-like sub-family belongs to the SF1 superfamily, and includes a group of enzymes involved in RNA metabolism centered in processes like splicing or nonsense-mediated decay. The SF2 superfamily includes five different sub-families of RNA helicases: DEAD-box helicases, DEAH-RHA helicases, RIG-I like proteins, Ski2-like proteins and the NS3/NPH-II subfamily. SF1 and SF2 RNA helicases have other variable accessory domains located around their structural cores which frequently contain specific additional functionalities such as DNA-binding, protein-binding or oligomerization. Structure-function relationships of the most widely-studied families of RNA helicases: the DEAD-box, RIG-I-like and viral NS3 classes, overview. Enzyme NS3 falls within NS3/NPH-II subfamily of SF2 helicase superfamily
evolution
the RNA helicase ubiquitous group of proteins is found in all the kingdoms of life, ranging from viruses to mammals, and it is closely related to DNA helicases. RNA helicases are included in five of the six nucleic acid helicase superfamilies. RNA helicases belonging to superfamilies SF3, SF4, and SF5 are oligomeric proteins (mostly hexamers), being typically encoded by genomes of viruses or bacteria. Superfamilies SF1 and SF2 of RNA helicases are non-oligomeric proteins, containing a conserved bi-lobular core composed by two RecA-like domains as a central structure. Several sub-families of RNA helicases are also defined on the basis of their sequence conservation and biological activity. Human RNA helicases are included in five different sub-families: Upf1-like, DEAD-box, DEAH-RHA, RIG-I like and Ski2-like proteins. The Upf1-like sub-family belongs to the SF1 superfamily, and includes a group of enzymes involved in RNA metabolism centered in processes like splicing or nonsense-mediated decay. The SF2 superfamily includes five different sub-families of RNA helicases: DEAD-box helicases, DEAH-RHA helicases, RIG-I like proteins, Ski2-like proteins and the NS3/NPH-II subfamily. SF1 and SF2 RNA helicases have other variable accessory domains located around their structural cores which frequently contain specific additional functionalities such as DNA-binding, protein-binding or oligomerization. Structure-function relationships of the most widely-studied families of RNA helicases: the DEAD-box, RIG-I-like and viral NS3 classes, overview. Enzyme NS3 falls within NS3/NPH-II subfamily of SF2 helicase superfamily
evolution
the RNA helicase ubiquitous group of proteins is found in all the kingdoms of life, ranging from viruses to mammals, and it is closely related to DNA helicases. RNA helicases are included in five of the six nucleic acid helicase superfamilies. RNA helicases belonging to superfamilies SF3, SF4, and SF5 are oligomeric proteins (mostly hexamers), being typically encoded by genomes of viruses or bacteria. Superfamilies SF1 and SF2 of RNA helicases are non-oligomeric proteins, containing a conserved bi-lobular core composed by two RecA-like domains as a central structure. Several sub-families of RNA helicases are also defined on the basis of their sequence conservation and biological activity. Human RNA helicases are included in five different sub-families: Upf1-like, DEAD-box, DEAH-RHA, RIG-I like and Ski2-like proteins. The Upf1-like sub-family belongs to the SF1 superfamily, and includes a group of enzymes involved in RNA metabolism centered in processes like splicing or nonsense-mediated decay. The SF2 superfamily includes five different sub-families of RNA helicases: DEAD-box helicases, DEAH-RHA helicases, RIG-I like proteins, Ski2-like proteins and the NS3/NPH-II subfamily. SF1 and SF2 RNA helicases have other variable accessory domains located around their structural cores which frequently contain specific additional functionalities such as DNA-binding, protein-binding or oligomerization. Structure-function relationships of the most widely-studied families of RNA helicases: the DEAD-box, RIG-I-like and viral NS3 classes, overview
evolution
the RNA helicase ubiquitous group of proteins is found in all the kingdoms of life, ranging from viruses to mammals, and it is closely related to DNA helicases. RNA helicases are included in five of the six nucleic acid helicase superfamilies. RNA helicases belonging to superfamilies SF3, SF4, and SF5 are oligomeric proteins (mostly hexamers), being typically encoded by genomes of viruses or bacteria. Superfamilies SF1 and SF2 of RNA helicases are non-oligomeric proteins, containing a conserved bi-lobular core composed by two RecA-like domains as a central structure. Several sub-families of RNA helicases are also defined on the basis of their sequence conservation and biological activity. Human RNA helicases are included in five different sub-families: Upf1-like, DEAD-box, DEAH-RHA, RIG-I like and Ski2-like proteins. The Upf1-like sub-family belongs to the SF1 superfamily, and includes a group of enzymes involved in RNA metabolism centered in processes like splicing or nonsense-mediated decay. The SF2 superfamily includes five different sub-families of RNA helicases: DEAD-box helicases, DEAH-RHA helicases, RIG-I like proteins, Ski2-like proteins and the NS3/NPH-II subfamily. SF1 and SF2 RNA helicases have other variable accessory domains located around their structural cores which frequently contain specific additional functionalities such as DNA-binding, protein-binding or oligomerization. Structure-function relationships of the most widely-studied families of RNA helicases: the DEAD-box, RIG-I-like and viral NS3 classes, overview. RIG-I falls within the Dicer-RIG-I clade of the superfamily 2 helicases
evolution
the RNA helicase ubiquitous group of proteins is found in all the kingdoms of life, ranging from viruses to mammals, and it is closely related to DNA helicases. RNA helicases are included in five of the six nucleic acid helicase superfamilies. RNA helicases belonging to superfamilies SF3, SF4, and SF5 are oligomeric proteins (mostly hexamers), being typically encoded by genomes of viruses or bacteria. Superfamilies SF1 and SF2 of RNA helicases are non-oligomeric proteins, containing a conserved bi-lobular core composed by two RecA-like domains as a central structure. Several sub-families of RNA helicases are also defined on the basis of their sequence conservation and biological activity. The Upf1-like sub-family belongs to the SF1 superfamily, and includes a group of enzymes involved in RNA metabolism centered in processes like splicing or nonsense-mediated decay. The SF2 superfamily includes five different sub-families of RNA helicases: DEAD-box helicases, DEAH-RHA helicases, RIG-I like proteins, Ski2-like proteins and the NS3/NPH-II subfamily. SF1 and SF2 RNA helicases have other variable accessory domains located around their structural cores which frequently contain specific additional functionalities such as DNA-binding, protein-binding or oligomerization. Structure-function relationships of the most widely studied families of RNA helicases: the DEAD-box, RIG-I-like and viral NS3 classes, detailed overview
evolution
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the RNA helicase ubiquitous group of proteins is found in all the kingdoms of life, ranging from viruses to mammals, and it is closely related to DNA helicases. RNA helicases are included in five of the six nucleic acid helicase superfamilies. RNA helicases belonging to superfamilies SF3, SF4, and SF5 are oligomeric proteins (mostly hexamers), being typically encoded by genomes of viruses or bacteria. Superfamilies SF1 and SF2 of RNA helicases are non-oligomeric proteins, containing a conserved bi-lobular core composed by two RecA-like domains as a central structure. Several sub-families of RNA helicases are also defined on the basis of their sequence conservation and biological activity. The Upf1-like sub-family belongs to the SF1 superfamily, and includes a group of enzymes involved in RNA metabolism centered in processes like splicing or nonsense-mediated decay. The SF2 superfamily includes five different sub-families of RNA helicases: DEAD-box helicases, DEAH-RHA helicases, RIG-I like proteins, Ski2-like proteins and the NS3/NPH-II subfamily. SF1 and SF2 RNA helicases have other variable accessory domains located around their structural cores which frequently contain specific additional functionalities such as DNA-binding, protein-binding or oligomerization. Structure-function relationships of the most widely studied families of RNA helicases: the DEAD-box, RIG-I-like and viral NS3 classes, detailed overview
evolution
binding of the Prp8 Jab1 C-terminal tail at the Brr2 RNA binding tunnel is evolutionarily conserved
evolution
Thermochaetoides thermophila
binding of the Prp8 Jab1 C-terminal tail at the Brr2 RNA binding tunnel is evolutionarily conserved
evolution
Brr2 is an RNA helicase belonging to the Ski2-like subfamily
evolution
CshA is a DEAD-box RNA helicase that belongs to the DExD/H-box family of proteins, which generally have an RNA-dependent ATPase activity
evolution
DDX5 (p68) and DDX17 (p72) belong to the large family of evolutionarily conserved DEAD box RNA helicases. The regulatory activity of DDX5 and DDX17 in transcription is conserved throughout evolution. Possible evolutionary divergence of the insulation process between drosophila and mammals
evolution
DDX5 (p68) and DDX17 (p72) belong to the large family of evolutionarily conserved DEAD box RNA helicases. The regulatory activity of DDX5 and DDX17 in transcription is conserved throughout evolution. Possible evolutionary divergence of the insulation process between drosophila and mammals
evolution
DDX5 (p68) and DDX17 (p72) belong to the large family of evolutionarily conserved DEAD box RNA helicases. The regulatory activity of DDX5 and DDX17 in transcription is conserved throughout evolution. Possible evolutionary divergence of the insulation process between drosophila and mammals
evolution
DDX5 (p68) and DDX17 (p72) belong to the large family of evolutionarily conserved DEAD box RNA helicases.The regulatory activity of DDX5 and DDX17 in transcription is conserved throughout evolution. Possible evolutionary divergence of the insulation process between drosophila and mammals
evolution
DEAD-box proteins belong to a ubiquitous family of RNA helicases, which are widely found from prokaryotes to eukaryotes and participate in multiple cellular processes, such as premRNA splicing, translation initiation, modulating RNA-protein complexes, RNA decay, and ribosome biogenesis. Sequence alignment and architecture of different DEAD-Box proteins, overview
evolution
DEAD-box proteins comprise the largest family of RNA helicases in plants, and exist in most organisms. They possess 12 conserved motifs that are involved in ATPase, helicase, and RNA binding activities, and participate in a variety of RNA-associated events from transcription to RNA decay. Some DEAD-box proteins are involved in the regulation of plant growth and development through ribosome biogenesis. Phylogenetic analysis, and evolutionary and functional relationships of AtRH7. AtRH7 belongs to a family whose members are involved in rRNA and mRNA processing. AtRH7 shares a conserved function with Escherichia coli enzyme CsdA under cold conditions
evolution
DHX9 belongs to the DExH/RHA family of helicase superfamily 2
evolution
Thermochaetoides thermophila
helicase Prp43 is an outstanding member of the DEAH-box subfamily since it has implications in different substantive cellular processes
evolution
ISE2 is a non-canonical Ski2-like RNA helicase that represents a separate sub-clade unique to green photosynthetic organisms. ISE2's evolutionary conservation may be explained by its numerous roles in regulating chloroplast gene expression
evolution
overall RNA binding mode is conserved between DHX8 and related SF2 helicases
evolution
RNA helicase A (RHA) as a member of the DExH/D-box subgroup of helicase superfamily II
evolution
RNA helicase p68 or DEAD (Asp-Glu-Ala-Asp) box polypeptide 5 (DDX5) is a unique member of the highly conserved protein family, which is involved in a broad spectrum of biological processes, including transcription, translation, precursor messenger RNA processing or alternative splicing, and microRNA (miRNA) processing
evolution
SF2 helicases can be grouped into 5 families, 3 of which are represented among the spliceosomal remodeling enzymes: 3 DEAD box proteins (Prp5, Sup2/UAP56, Prp28) act during initial spliceosome assembly and activation, a single Ski2-like helicase (Brr2) is involved in spliceosome activation and 4 DEAH/RHA enzymes (Prp2, Prp16, Prp22, Prp43) are required during spliceosome activation, catalysis and disassembly
evolution
SF2 helicases can be grouped into 5 families, 3 of which are represented among the spliceosomal remodeling enzymes: 3 DEAD box proteins (Prp5, Sup2/UAP56, Prp28) act during initial spliceosome assembly and activation, a single Ski2-like helicase (Brr2) is involved in spliceosome activation and 4 DEAH/RHA enzymes (Prp2, Prp16, Prp22, Prp43) are required during spliceosome activation, catalysis and disassembly
evolution
the enzyme is a member of the DEAD box family of RNA helicases that have roles in mRNA degradation and ribosome biogenesis, an additional role in gene regulation is determined for bacteria. DEAD box helicases are thought to promote translation by enhancing ribosomal recruitment
evolution
UPF1 exists as two alternatively-spliced isoforms in mammals, which differ only in the length of this regulatory loop
evolution
-
the enzyme is a member of the DEAD box family of RNA helicases that have roles in mRNA degradation and ribosome biogenesis, an additional role in gene regulation is determined for bacteria. DEAD box helicases are thought to promote translation by enhancing ribosomal recruitment
-
evolution
Thermochaetoides thermophila IMI 039719
-
helicase Prp43 is an outstanding member of the DEAH-box subfamily since it has implications in different substantive cellular processes
-
evolution
Thermochaetoides thermophila IMI 039719
-
binding of the Prp8 Jab1 C-terminal tail at the Brr2 RNA binding tunnel is evolutionarily conserved
-
evolution
Thermochaetoides thermophila DSM 1495
-
helicase Prp43 is an outstanding member of the DEAH-box subfamily since it has implications in different substantive cellular processes
-
evolution
Thermochaetoides thermophila DSM 1495
-
binding of the Prp8 Jab1 C-terminal tail at the Brr2 RNA binding tunnel is evolutionarily conserved
-
evolution
-
the enzyme is a member of the DEAD box family of RNA helicases that have roles in mRNA degradation and ribosome biogenesis, an additional role in gene regulation is determined for bacteria. DEAD box helicases are thought to promote translation by enhancing ribosomal recruitment
-
evolution
-
the enzyme is a member of the DEAD box family of RNA helicases that have roles in mRNA degradation and ribosome biogenesis, an additional role in gene regulation is determined for bacteria. DEAD box helicases are thought to promote translation by enhancing ribosomal recruitment
-
evolution
-
CshA is a DEAD-box RNA helicase that belongs to the DExD/H-box family of proteins, which generally have an RNA-dependent ATPase activity
-
evolution
-
ISE2 is a non-canonical Ski2-like RNA helicase that represents a separate sub-clade unique to green photosynthetic organisms. ISE2's evolutionary conservation may be explained by its numerous roles in regulating chloroplast gene expression
-
evolution
-
the enzyme is a member of the DEAD box family of RNA helicases that have roles in mRNA degradation and ribosome biogenesis, an additional role in gene regulation is determined for bacteria. DEAD box helicases are thought to promote translation by enhancing ribosomal recruitment
-
evolution
-
the enzyme is a member of the DEAD box family of RNA helicases that have roles in mRNA degradation and ribosome biogenesis, an additional role in gene regulation is determined for bacteria. DEAD box helicases are thought to promote translation by enhancing ribosomal recruitment
-
evolution
-
the enzyme is a member of the DEAD box family of RNA helicases that have roles in mRNA degradation and ribosome biogenesis, an additional role in gene regulation is determined for bacteria. DEAD box helicases are thought to promote translation by enhancing ribosomal recruitment
-
evolution
-
SF2 helicases can be grouped into 5 families, 3 of which are represented among the spliceosomal remodeling enzymes: 3 DEAD box proteins (Prp5, Sup2/UAP56, Prp28) act during initial spliceosome assembly and activation, a single Ski2-like helicase (Brr2) is involved in spliceosome activation and 4 DEAH/RHA enzymes (Prp2, Prp16, Prp22, Prp43) are required during spliceosome activation, catalysis and disassembly
-
evolution
Thermochaetoides thermophila CBS 144.50
-
helicase Prp43 is an outstanding member of the DEAH-box subfamily since it has implications in different substantive cellular processes
-
evolution
Thermochaetoides thermophila CBS 144.50
-
binding of the Prp8 Jab1 C-terminal tail at the Brr2 RNA binding tunnel is evolutionarily conserved
-
evolution
-
CshA is a DEAD-box RNA helicase that belongs to the DExD/H-box family of proteins, which generally have an RNA-dependent ATPase activity
-
evolution
-
the enzyme is a member of the DEAD box family of RNA helicases that have roles in mRNA degradation and ribosome biogenesis, an additional role in gene regulation is determined for bacteria. DEAD box helicases are thought to promote translation by enhancing ribosomal recruitment
-
malfunction
conditional ablation of Supv3L1 in adult mice leads to premature aging phenotypes including loss of muscle mass and adipose tissue and severe skin abnormalities
malfunction
-
knockdown of endogenous RHA significantly reduces the interaction of RNA polymerase II with beta-actin
malfunction
-
mutation of the crhR gene by replacement with a spectinomycin-resistance gene cassette. The resultant DELTAcrhR mutant exhibits a phenotype of slow growth at low temperatures. CrhR regulates the low-temperature-inducible expression of the heat-shock proteins groEL1 and groEL2, which, in turn, may be essential for acclimatization of Synechocystis cells to low temperatures
malfunction
-
by using wild-type, helps mutant and overexpression lines of Arabidopsis, it is shown that, in the low-K+ condition, AtHELPS inhibits Arabidopsis seed germination via decreased K+ influx into roots. Expression of AKT1, CBL1, CBL9 and CIPK23 is regulated by AtHELPS under low-K+ stress
malfunction
-
crhR deletion results in failure to cold acclimate: there is reduced growth at 24°C and marked impairment of growth at 20°C compared to wild-type. Using a proteomic approach differentially expressed proteins are identified
malfunction
DDX3 knockdown blocks the shuttling of DDX5 to the nucleus
malfunction
-
disruption of the hrpA gene results in a complete loss in the ability of the spirochetes to infect mice by needle inoculation. Protein expression analysis show a total of 187 differentially regulated proteins in an hrpA background: 90 downregulated and 97 upregulated. 42 of the 90 downregulated and 65 of the 97 upregulated proteins are not regulated under any conditions by the previously reported regulators in Borrelia burgdorferi (bosR, rrp2, rpoN, rpoS or rrp1)
malfunction
-
knockdown of RH22 expression results in virescent seedlings with clear defects in chloroplast ribosomal RNA accumulation. The precursors of 23S and 4.5S, but not 16S, rRNA accumulate in rh22 mutants
malfunction
-
knockdown of RHA prevents formation of polysomes on collagen mRNAs and dramatically reduces synthesis of collagen protein, without affecting the level of the mRNAs
malfunction
-
RHAU knockdown by small interfering RNA (siRNA) results in a significant reduction in average telomere lengths supporting an impact of RHAU on telomerase function
malfunction
-
when Vasa accumulation is attenuated by injection of Vasa morpholino antisense oligonucleotide in the early embryo, the cells show a severe delay in their cell cycle progression in a dose-dependent manner and lack normal spindles even following chromosome condensation
malfunction
-
when Vasa accumulation is attenuated by injection of Vasa morpholino antisense oligonucleotide in the early embryo, the cells show a severe delay in their cell cycle progression in a dose-dependent manner and lack normal spindles even following chromosome condensation
malfunction
-
when Vasa accumulation is attenuated by injection of Vasa morpholino antisense oligonucleotide in the early embryo, the cells show a severe delay in their cell cycle progression in a dose-dependent manner and lack normal spindles even following chromosome condensation
malfunction
-
wild type Synechocystis cells acclimatize to low temperature by energy redistribution (state transitions) and regulating the PSI and PSII stoichiometry. In contrast the mutant cells deficient in CrhR fail to operate state transitions and are unable to regulate the photosystem stoichiometry. Mutant cells deficient in CrhR can not acclimatize to low temperature
malfunction
a reduction in the phosphorylation of endogenous UPF1 protein is observed upon DHX34 depletion. The levels of UPF1 phosphorylation are rescued upon the expression of an shRNA-resistant wild-type DHX34 construct, but not by the ATPase-deficient DHX34 mutants (K191S or D279A), which affect ATP binding or ATP hydrolysis, respectively. Overexpression of DHX34 affects the recruitment of SMG9, a subunit of the SMG1c complex, as well as the DHX34-dependent recruitment of UPF2 and eIF4A3
malfunction
an enzyme-defective strain is less motile due to downregulation of the major subunit of the flagellum, FlaA, caused by decreased flaA expression. Absence of helicase Lmo1722 decreases the fraction of 50S ribosomal subunits and mature 70S ribosomes and affects the processing of the 23S precursor rRNA. The ribosomal profile can be restored to wild-type levels in a DELTAlmo1722 strain expressing enzyme Lmo1722. Enzyme Lmo1722 lacking the C-terminus shows a reduced affinity for the 50S and 70S fractions
malfunction
AtRH3 null mutants are embryo lethal, whereas a weak allele results in pale-green seedlings with defects in splicing of several group II introns and rRNA maturation as well as reduced levels of assembled ribosomes,phenotype overview
malfunction
knockdown of several RNA helicases influences lifespan through the insulin/insulin-like growth factor 1 signaling pathway. Up-regulation of a large subset of genes in daf-2 mutants is affected by mutation hel-1
malfunction
a selected subset of RNAs is significantly stabilised in absence of the RNA helicase
malfunction
a severe growth defect is observed in the cshA mutant compared with the parent when grown at 25°C but not at 37°C. Activation of MazFsa in the cshA mutant results in lower CFU per milliliter accompanied by a precipitous drop in viability (about 40%) compared to those of the parent and complemented strains. NanoString analysis reveals diminished expression of a small number of mRNAs and 22 small RNAs (sRNAs) in the cshA mutant versus the parent upon MazFsa induction, thus implying protection of these RNAs by CshA. In the case of the sRNA teg049 within the sarA locus, the protective effect is likely due to transcript stability as revealed by reduced half-life in the cshA mutant versus the parent. Mutation of cshA affects growth and cell viability
malfunction
an ATPase-deficient Aquarius mutant hinders splicing
malfunction
breaking the sequence of the interdomain peptide linker and inserting the 23 amino acids peptide segment causes a decrease in binding affinity, likely as a consequence of formation of non-native interaction between the insert peptide and the RNA molecule or other regions of the protein and not a consequence of disrupting native interactions between the DbpA RNA binding domain and the interdomain linker. The peptide extension is not effecting the formation of the proper ATP pocket, but the ATP turnover rate is affected by the peptide extension. Although the ATP turnover of the extended DbpA is reduced when compared to wild-type DbpA, extended DbpA is a much more efficient enzyme than many members of DEAD-box family of proteins. The reduction on the ATP turnover of the extended DbpA is a consequence of its decrease in binding affinity for RNA. The extension of the interdomain linker region has no effect on the ability of DbpA to perform its helicase function. Thus, the physical connection of DbpA RNA binding domain to the catalytic core is unimportant for the helicase activity of DbpA, suggesting the DbpA protein is a region-specific enzyme, which would unwind any double-helix substrate near hairpin 92
malfunction
C-terminal mutants of DED1 are defective in downregulating transxadlation following TORC1 inhibition using rapamycin. EIF4G1 normally dissociates from translation complexes and is degraded, and this process is attenuated in mutant cells. The repressive function of overexpressed Ded1 is partially dependent on the Ded1 C-terminal domain, which is a predicted low-complexity sequence that lies outside of the core helicase domains. Deletion of this domain (amino acids 536-604) substantially rescues growth inhibition on overexpression. Deletion of the Ded1 C-terminus confers resistance against small molecule growth inhibitor rapamycin, a specific inhibitor of TORC1
malfunction
chloroplasts in leaves with reduced ISE2 expression show reduced thylakoid contents and increased stromal volume, indicative of defective development. Embryonic-lethal phenotype of Arabidopsis ise2 mutants. Changes observed in RNA editing in tissues with decreased ISE2 levels (ISE2-SUP leaves) are due to the specific effects of ISE2 and not due to general chlorosis, RNA editing is also measured in chlorotic leaves resulting from disruption of other genes
malfunction
ddx27 mutant zebrafish show skeletal muscle abnormalities and growth defects, but without significant expression changes in muscle progenitor cell markers, pax3 and pax7 during the embryonic stage. Significant downregulation of both pax7a and b is observed during the larval stage in ddx27 mutant zebrafish, and reduced Pax7-positive cell proliferation and impaired regeneration in Ddx27 deficiency. Concurrently, with a downregulation of pax3 and pax7a/b, high expression of myoD, myf5 and desmin in mutant muscles is observed suggesting a premature activation of the myogenic program in Ddx27 deficiency. Skeletal muscle hypotrophy and precocious differentiation occur in Ddx27 deficiency, and reduced contractile strength and prolonged muscle relaxation in Ddx27-deficient skeletal muscles. Ddx27 deficiency phenotype, detailed overview. Ddx27 deficiency perturbs the translation of specific subset of mRNA repertoires
malfunction
embryonic stem cells (ESCs) depleted of DHX9 are unable to differentiate, and this phenotype is reverted by the addition of pRNA, whereas providing IGS-rRNA and pRNA mutants deficient for TIP5 binding are not sufficient. Knockdown of TIP5 does not affect DHX9 levels. NIH 3T3 cells depleted of DHX9 show a reduction in rRNA gene silencing
malfunction
knockout mutant lines display several morphological alterations such as disturbed vein pattern, pointed first true leaves, and short roots, which resemble ribosome-related mutants of Arabidopsis thaliana. In addition, aberrant floral development as also observed in rh7 mutants. When the mutants are germinated at low temperature (12°C), both radicle and first leaf emergence are severely delayed, after exposure of seedlings to a long period of cold, the mutants develop aberrant, fewer, and smaller leaves. RNA blots and circular RT-PCR reveal that 35S and 18S rRNA precursors accumulate to higher levels in the mutants than in wild-type under both normal and cold conditions, suggesting the mutants are partially impaired in pre-rRNA processing
malfunction
mice lacking DDX3X during hematopoiesis show an altered leukocyte composition in bone marrow and spleen and a striking inability to combat infection with Listeria monocytogenes. Mice lacking DDX3X in the hematopoietic system show alterations of bone marrow and splenic cell populations. Alterations in innate immune responses result from decreased effector cell availability and function as well as a sex-dependent impairment of cytokine synthesis. Production of important cytokines such as IL12 or IFNgamma is reduced, DDX3X-deficient macrophages show reduced ability to restrict Listeria monocytogenes growth. Owing to partial redundancy with its close Y chromosomal homologue, DDX3Y, the observed effects differ between mouse sexes. DDX3Y, either alone or together with additional Y-chromosomal genes, partially compensates for the loss of the Ddx3x gene, as homozygous female cells and mice show more severe loss-of-function phenotypes
malfunction
p68 can bind to the acetyl transferase p300 and facilitate the p300-mediated acetylation, irregular activation of p68 disrupts the binding, which leads to the interaction with HDACs. Silencing p68 by shRNAs inhibits the proliferation of four distinct breast cancer cell lines (MDA-MB-453, SK-BR-3, EFM19, and ZR-75-1). Knockdown of the DDX5 in the breast cancer cell lines whose expansion is required for its upregulation exerts more inhibitory effects compared with those cell lines whose expansion does not require DDX5. Abnormal expression of p68 in tumor may be in part due to c-Myc-dependent Wnt signaling, overview. Silencing of either beta-catenin or c-Myc leads to downregulation of the Wnt3a-dependent p68 overexpression
malfunction
ribose-phosphate backbone lesions on both strands of the nucleic acids, especially on the 3' overhang of the loading strand, affect RHA unwinding significantly
malfunction
the aberrant expression of DDX5 and/or DDX17 contributes to pathologies such as cancer
malfunction
the aberrant expression of DDX5 and/or DDX17 contributes to pathologies such as cancer
malfunction
the aberrant expression of DDX5 and/or DDX17 contributes to pathologies such as cancer
malfunction
the aberrant expression of DDX5 and/or DDX17 contributes to pathologies such as cancer. DDX17 depletion is associated with a decrease of breast cancer tumor characteristics (e.g. colony formation), highlighting its importance in breast tumorigenesis
malfunction
the affinity for RNA is over 90fold weaker in the absence of nucleotide and in the presence of ADP, the RNA affinity is too weak to determine. These results indicate that DHX8-mediated disruption of RNA interactions occurs through a series of alternating strong and weak RNA binding events controlled by ATP hydrolysis. Both full-length fl-DHX8 and truncated DHX8DELAT547 preferentially bind the purine nucleotides ADP and GDP, but are also able to bind CDP, TDP and UDP. DHX8 is an RNA-specific helicase by showing that a poly(dA)10 DNA strand cannot displace Cy5-poly(A)10 from DHX8 in the presence of ADP-AlFx. The displacement of the probe with poly(A)10, poly(C)10, poly(G)10 and poly(U)10 RNA indicates that DHX8 has a preference for binding adenine-rich sequences as the rank ascending order of IC50 values is poly (A)10, poly(U)10, poly(C)10, poly(G)10
malfunction
transposon disruptions within gene PA2840, which encodes a homolog of the Escherichia coli RNA-helicase DeaD, significantly reduces Pseudomonas aeruginosa type III secretion system (T3SS) gene expression, the activity of an exsA translational fusion is reduced in a deaD mutant. In addition, exsA expression in trans fails to restore T3SS gene expression in a deaD mutant
malfunction
two viable mutant lines are generated by p-element insertion in the regulatory region, belle cap-1 and belle EY08943, flies are entrained for 3 days in light dark cycles at constant temperature (23°C) followed by 7 days of constant darkness. Either mutant exhibits an impairment of the locomotor behavior: in light-darkness (LD) conditions, both lines presented the canonical bimodal profile, but a severe loss of the morning anticipation of the locomotor activity is displayed. A high percentage of flies show also an arrhythmic behavior in constant darkness (DD), although no defects are monitored concerning the period, which is comparable to wild-type. Mutant lines show defects in some clusters of neurons. Under LD conditions, belle cap-1 flies exhibit a significant reduction of oscillation amplitude in both s-LNvs and l-LNvs, particularly marked at ZT0. Similarly, in constant darkness, a general decrease of PER staining is observed compared to wild-type, which is particularly enhanced during the subjective night/beginning of the subjective day. RNAi against belle in the photoreceptor cells (GMR-Gal4 and ninaE-Gal4) does not affect either vitality or behavior. Knockdown of belle with the pan-glial driver repo-Gal4 and lama-Gal4, a driver for glial precursor cells, lamina precursor cells and lamina neurons causes developmental lethality
malfunction
-
transposon disruptions within gene PA2840, which encodes a homolog of the Escherichia coli RNA-helicase DeaD, significantly reduces Pseudomonas aeruginosa type III secretion system (T3SS) gene expression, the activity of an exsA translational fusion is reduced in a deaD mutant. In addition, exsA expression in trans fails to restore T3SS gene expression in a deaD mutant
-
malfunction
-
a selected subset of RNAs is significantly stabilised in absence of the RNA helicase
-
malfunction
-
a severe growth defect is observed in the cshA mutant compared with the parent when grown at 25°C but not at 37°C. Activation of MazFsa in the cshA mutant results in lower CFU per milliliter accompanied by a precipitous drop in viability (about 40%) compared to those of the parent and complemented strains. NanoString analysis reveals diminished expression of a small number of mRNAs and 22 small RNAs (sRNAs) in the cshA mutant versus the parent upon MazFsa induction, thus implying protection of these RNAs by CshA. In the case of the sRNA teg049 within the sarA locus, the protective effect is likely due to transcript stability as revealed by reduced half-life in the cshA mutant versus the parent. Mutation of cshA affects growth and cell viability
-
malfunction
-
transposon disruptions within gene PA2840, which encodes a homolog of the Escherichia coli RNA-helicase DeaD, significantly reduces Pseudomonas aeruginosa type III secretion system (T3SS) gene expression, the activity of an exsA translational fusion is reduced in a deaD mutant. In addition, exsA expression in trans fails to restore T3SS gene expression in a deaD mutant
-
malfunction
-
a severe growth defect is observed in the cshA mutant compared with the parent when grown at 25°C but not at 37°C. Activation of MazFsa in the cshA mutant results in lower CFU per milliliter accompanied by a precipitous drop in viability (about 40%) compared to those of the parent and complemented strains. NanoString analysis reveals diminished expression of a small number of mRNAs and 22 small RNAs (sRNAs) in the cshA mutant versus the parent upon MazFsa induction, thus implying protection of these RNAs by CshA. In the case of the sRNA teg049 within the sarA locus, the protective effect is likely due to transcript stability as revealed by reduced half-life in the cshA mutant versus the parent. Mutation of cshA affects growth and cell viability
-
malfunction
-
transposon disruptions within gene PA2840, which encodes a homolog of the Escherichia coli RNA-helicase DeaD, significantly reduces Pseudomonas aeruginosa type III secretion system (T3SS) gene expression, the activity of an exsA translational fusion is reduced in a deaD mutant. In addition, exsA expression in trans fails to restore T3SS gene expression in a deaD mutant
-
malfunction
-
chloroplasts in leaves with reduced ISE2 expression show reduced thylakoid contents and increased stromal volume, indicative of defective development. Embryonic-lethal phenotype of Arabidopsis ise2 mutants. Changes observed in RNA editing in tissues with decreased ISE2 levels (ISE2-SUP leaves) are due to the specific effects of ISE2 and not due to general chlorosis, RNA editing is also measured in chlorotic leaves resulting from disruption of other genes
-
malfunction
-
transposon disruptions within gene PA2840, which encodes a homolog of the Escherichia coli RNA-helicase DeaD, significantly reduces Pseudomonas aeruginosa type III secretion system (T3SS) gene expression, the activity of an exsA translational fusion is reduced in a deaD mutant. In addition, exsA expression in trans fails to restore T3SS gene expression in a deaD mutant
-
malfunction
-
transposon disruptions within gene PA2840, which encodes a homolog of the Escherichia coli RNA-helicase DeaD, significantly reduces Pseudomonas aeruginosa type III secretion system (T3SS) gene expression, the activity of an exsA translational fusion is reduced in a deaD mutant. In addition, exsA expression in trans fails to restore T3SS gene expression in a deaD mutant
-
malfunction
-
transposon disruptions within gene PA2840, which encodes a homolog of the Escherichia coli RNA-helicase DeaD, significantly reduces Pseudomonas aeruginosa type III secretion system (T3SS) gene expression, the activity of an exsA translational fusion is reduced in a deaD mutant. In addition, exsA expression in trans fails to restore T3SS gene expression in a deaD mutant
-
malfunction
-
C-terminal mutants of DED1 are defective in downregulating transxadlation following TORC1 inhibition using rapamycin. EIF4G1 normally dissociates from translation complexes and is degraded, and this process is attenuated in mutant cells. The repressive function of overexpressed Ded1 is partially dependent on the Ded1 C-terminal domain, which is a predicted low-complexity sequence that lies outside of the core helicase domains. Deletion of this domain (amino acids 536-604) substantially rescues growth inhibition on overexpression. Deletion of the Ded1 C-terminus confers resistance against small molecule growth inhibitor rapamycin, a specific inhibitor of TORC1
-
malfunction
-
an enzyme-defective strain is less motile due to downregulation of the major subunit of the flagellum, FlaA, caused by decreased flaA expression. Absence of helicase Lmo1722 decreases the fraction of 50S ribosomal subunits and mature 70S ribosomes and affects the processing of the 23S precursor rRNA. The ribosomal profile can be restored to wild-type levels in a DELTAlmo1722 strain expressing enzyme Lmo1722. Enzyme Lmo1722 lacking the C-terminus shows a reduced affinity for the 50S and 70S fractions
-
malfunction
-
transposon disruptions within gene PA2840, which encodes a homolog of the Escherichia coli RNA-helicase DeaD, significantly reduces Pseudomonas aeruginosa type III secretion system (T3SS) gene expression, the activity of an exsA translational fusion is reduced in a deaD mutant. In addition, exsA expression in trans fails to restore T3SS gene expression in a deaD mutant
-
metabolism
UV cross-linking experiments show that both RNA helicase proteins are involved in mRNP metabolism and that DDX3 affects the shuttling of DDX5 to the nucleus
metabolism
RNA helicase DHX34 activates nonsense-mediated decay (NMD), a surveillance mechanism that degrades aberrant mRNAs. A complex comprising SMG1, UPF1, and the translation termination factors eRF1 and eRF3 (SURF) is assembled in the vicinity of a premature termination codon. Subsequently, an interaction with UPF2, UPF3b, and the exon junction complex induces the formation of the decay-inducing complex (DECID) and triggers NMD. The central NMD factor is the ATP-dependent RNA helicase UPF1
metabolism
analysis of lncRNA biogenesis during development and support of a model in which the state of rRNA gene chromatin is part of the regulatory network that controls exit from pluripotency and initiation of differentiation pathways. Critical role of pRNA biogenesis in the establishment of rRNA gene heterochromatin. DHX9 is required for the formation of heterochromatin at rRNA genes through processing of IGS-rRNA into pRNA
metabolism
DeaD RNA-helicase regulates ExsA synthesis and the T3SS expression. DeaD-based regulation of T3SS gene expression does not involve the Gac/Rsm system
metabolism
Ded1 activity plays an important role in promoting translation repression and adaptation to stress conditions. Ded1 activity is essential for translaxadtion initiation, but above a certain threshold Ded1 becomes inhibitory toward translation
metabolism
in Drosophila melanogaster, BELLE, a conserved DEAD-box RNA helicase playing important roles in reproductive capacity, is involved in the small RNA-mediated regulation associated to the piRNA pathway
metabolism
in the Neurospora crassa circadian core clock oscillator, FRH associates with FRQ and CK1a to form a repressor complex (FFC) that inhibits the positive-acting white collar transcription factors (WC-1 and WC-2) which form the white-collar complex (WCC)
metabolism
pivotal and sex-specific role for the heterosomal isoforms of the DEAD box RNA helicase DDX3 in the immune system. Mechanism of DDX3X action, redundancy with DDX3Y, overview
metabolism
protein and noncoding RNA partners of DDX5 and DDX17, DDX5/DDX17 and the regulation of gene insulation, overview. DDX5 and DDX17 can regulate alternative splicing through other mechanisms, via a direct effect on the local folding of their targeted transcripts or via the recruitment of RNA binding cofactors
metabolism
protein and noncoding RNA partners of DDX5 and DDX17, DDX5/DDX17 and the regulation of gene insulation, overview. DDX5 and DDX17 can regulate alternative splicing through other mechanisms, via a direct effect on the local folding of their targeted transcripts or via the recruitment of RNA binding cofactors
metabolism
protein and noncoding RNA partners of DDX5 and DDX17, overview. DDX5 and DDX17 can regulate alternative splicing through other mechanisms, via a direct effect on the local folding of their targeted transcripts or via the recruitment of RNA binding cofactors
metabolism
RNA helicase A (RHA) is involved in virtually all aspects of RNA metabolism
metabolism
role of RNA helicase Ddx27 in skeletal muscle homeostasis
metabolism
Thermochaetoides thermophila
the enzyme is a spliceosomal DEAD-box helicase which is involved in two steps of spliceosome assembly. It is required for the formation of the pre-catalytic spliceosome, which is ATP-dependent
metabolism
the enzyme is involved in the pre-mRNA splicing cycle by the spliceosome, reaction steps in processing, detailed overview. The most dramatic rearrangements occur during spliceosome activation, where the Prp28 helicase aids in the displacement of U1 snRNA from the 5SS,8,23,24 followed by Brr2 unwinding the U4 and U6 snRNAs and leading to displacement of U4 snRNA and U4/U6-bound proteins. Brr2 requires tight regulation
metabolism
the enzyme is involved in the pre-mRNA splicing cycle by the spliceosome, reaction steps in processing, detailed overview. The most dramatic rearrangements occur during spliceosome activation, where the Prp28 helicase aids in the displacement of U1 snRNA from the 5SS,8,23,24 followed by Brr2 unwinding the U4 and U6 snRNAs and leading to displacement of U4 snRNA and U4/U6-bound proteins. Brr2 requires tight regulation
metabolism
the RNA helicase UPF1 is a key component of the nonsense mediated mRNA decay (NMD) pathway
metabolism
the spliceosome's structural rearrangements are driven by eight conserved DExH/D-box RNA helicases that contain two RecA-like domains, which form a motor module required for ATP hydrolysis, RNA unwinding and coupling of these two processes. RNA helixadcases can have very diverse functions, including proofreading specific steps of pre-mRNA splicing. Most helicases also conxadtain specific accessory domains important for their regulation or task-specific function. The human spliceosome contains five addixadtional RNA helicases (Aquarius, SF3b125, elFAIII and DDX35 and Abstrakt). Multiple cross-links between Aquarius and hSyf1, hIsy1, CCDC16 or CypE, with the majority of the cross-linked residues located in domains or structural insertions specific for Aquarius, such as the ARM, pointer and thumb domains, and in the large insertions of the beta-barrel. The for intron-binding complex (IBC) is cross-linked to U2 SF3a and SF3b proteins, interaction partners of the IBC in the spliceosome. The Aquarius ARM domain is cross-linked to SF3b155
metabolism
the toxin MazFsa in Staphylococcus aureus is a sequence-specific endoribonuclease that cleaves the majority of the mRNAs in vivo but spares many essential mRNAs (e.g., secY mRNA) and, surprisingly, an mRNA encoding a regulatory protein (i.e., sarA mRNA). CshA likely stabilizes selective mRNAs and sRNAs in vivo and as a result enhances Staphylococcus aureus survival upon MazFsa induction during stress
metabolism
-
DeaD RNA-helicase regulates ExsA synthesis and the T3SS expression. DeaD-based regulation of T3SS gene expression does not involve the Gac/Rsm system
-
metabolism
-
the toxin MazFsa in Staphylococcus aureus is a sequence-specific endoribonuclease that cleaves the majority of the mRNAs in vivo but spares many essential mRNAs (e.g., secY mRNA) and, surprisingly, an mRNA encoding a regulatory protein (i.e., sarA mRNA). CshA likely stabilizes selective mRNAs and sRNAs in vivo and as a result enhances Staphylococcus aureus survival upon MazFsa induction during stress
-
metabolism
Thermochaetoides thermophila DSM 1495
-
the enzyme is a spliceosomal DEAD-box helicase which is involved in two steps of spliceosome assembly. It is required for the formation of the pre-catalytic spliceosome, which is ATP-dependent
-
metabolism
-
DeaD RNA-helicase regulates ExsA synthesis and the T3SS expression. DeaD-based regulation of T3SS gene expression does not involve the Gac/Rsm system
-
metabolism
-
the toxin MazFsa in Staphylococcus aureus is a sequence-specific endoribonuclease that cleaves the majority of the mRNAs in vivo but spares many essential mRNAs (e.g., secY mRNA) and, surprisingly, an mRNA encoding a regulatory protein (i.e., sarA mRNA). CshA likely stabilizes selective mRNAs and sRNAs in vivo and as a result enhances Staphylococcus aureus survival upon MazFsa induction during stress
-
metabolism
-
DeaD RNA-helicase regulates ExsA synthesis and the T3SS expression. DeaD-based regulation of T3SS gene expression does not involve the Gac/Rsm system
-
metabolism
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in the Neurospora crassa circadian core clock oscillator, FRH associates with FRQ and CK1a to form a repressor complex (FFC) that inhibits the positive-acting white collar transcription factors (WC-1 and WC-2) which form the white-collar complex (WCC)
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metabolism
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DeaD RNA-helicase regulates ExsA synthesis and the T3SS expression. DeaD-based regulation of T3SS gene expression does not involve the Gac/Rsm system
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metabolism
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DeaD RNA-helicase regulates ExsA synthesis and the T3SS expression. DeaD-based regulation of T3SS gene expression does not involve the Gac/Rsm system
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metabolism
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DeaD RNA-helicase regulates ExsA synthesis and the T3SS expression. DeaD-based regulation of T3SS gene expression does not involve the Gac/Rsm system
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metabolism
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Ded1 activity plays an important role in promoting translation repression and adaptation to stress conditions. Ded1 activity is essential for translaxadtion initiation, but above a certain threshold Ded1 becomes inhibitory toward translation
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metabolism
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the enzyme is involved in the pre-mRNA splicing cycle by the spliceosome, reaction steps in processing, detailed overview. The most dramatic rearrangements occur during spliceosome activation, where the Prp28 helicase aids in the displacement of U1 snRNA from the 5SS,8,23,24 followed by Brr2 unwinding the U4 and U6 snRNAs and leading to displacement of U4 snRNA and U4/U6-bound proteins. Brr2 requires tight regulation
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metabolism
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in the Neurospora crassa circadian core clock oscillator, FRH associates with FRQ and CK1a to form a repressor complex (FFC) that inhibits the positive-acting white collar transcription factors (WC-1 and WC-2) which form the white-collar complex (WCC)
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metabolism
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in the Neurospora crassa circadian core clock oscillator, FRH associates with FRQ and CK1a to form a repressor complex (FFC) that inhibits the positive-acting white collar transcription factors (WC-1 and WC-2) which form the white-collar complex (WCC)
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metabolism
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in the Neurospora crassa circadian core clock oscillator, FRH associates with FRQ and CK1a to form a repressor complex (FFC) that inhibits the positive-acting white collar transcription factors (WC-1 and WC-2) which form the white-collar complex (WCC)
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metabolism
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DeaD RNA-helicase regulates ExsA synthesis and the T3SS expression. DeaD-based regulation of T3SS gene expression does not involve the Gac/Rsm system
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metabolism
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in the Neurospora crassa circadian core clock oscillator, FRH associates with FRQ and CK1a to form a repressor complex (FFC) that inhibits the positive-acting white collar transcription factors (WC-1 and WC-2) which form the white-collar complex (WCC)
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physiological function
ATPase/helicase activity allows protein complex remodeling that dictates the balance between repressors and an activator of translation
physiological function
is a part of the homeostatic machinery that regulates the switch between cellular proliferation and differentiation
physiological function
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phosphorylation of p68 RNA helicase at Y593 upregulates transcription of the Snail1 gene. The phosphorylated p68 activates transcription of the Snail1 gene by promoting histone deacetylase dissociation from the Snail1 promoter. p68 interacts with the nuclear remodeling and deacetylation complex MBD3:Mi-2/NuRD. The DEAD-box RNA unwindase could potentially regulate gene expression by functioning as a protein displacer to modulate proteinprotein interactions at the chromatin-remodeling complex
physiological function
plays a critical role in the mitochondrial RNA surveillance and degradation machinery
physiological function
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the enzyme functions under cold stress conditions
physiological function
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the enzyme plays an essential role in pre-mRNA splicing. Mutation within hBrr2p can be linked to autosomal dominant retinitis pigmentosa
physiological function
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the enzyme plays an important role in linking beta-actin with RNA polymerase II and functions in gene transcription regulation
physiological function
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the protein plays a very important role in early organ development and maturation, function of the protein in transcriptional regulation and pre-mRNA splicing
physiological function
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the West Nile virus RNA helicase uses the energy derived from the hydrolysis of nucleotides to separate complementary strands of RNA
physiological function
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through its export/transport function as a component of mRNP (mRNAs that associate with ribonuclear particles) GRTH is essential to govern the structure of the chromatoid body in spermatids and to maintain systems that may participate in mRNA storage and their processing during spermatogenesis
physiological function
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translation of HIV-1 gag mRNA is reliant on the ATP-dependent helicase activity of RNA helicase A
physiological function
in vitro efficiency of L1917 intron splicing is significantly enhanced in the presence of a recombinant Coxiella RNA DEAD-box helicase relative to that of controls, suggesting that this enzyme may serve as an intron RNA splice facilitator in vivo
physiological function
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RH22 may function in the assembly of 50S ribosomal subunits in chloroplasts
physiological function
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RHA interacts with LARP6, which recruits RHA to the 5' UTR of collagen mRNAs. There, RHA activity is necessary for efficient formation of polysomes and a high level of collagen protein synthesis
physiological function
using an RNA affinity pulldown-coupled mass spectrometry approach DDX5/RNA helicase p68 is identified as an activator of tau exon 10 splicing. p68 regulates tau exon 10 splicing by interacting with the stem-loop region, destabilizing the stem structure, and facilitating U1snRNP binding to this 5' splice site
physiological function
DEAD-box RNA helicases play important roles in all types of processes in RNA metabolism. TaRH1 gene may participate in the plant stress response
physiological function
enzyme RHA plays multiple roles in cellular biology, some functions requiring its activity as a helicase while others as a protein scaffold. The oncogenic transcription factor EWS-FLI1 requires RHA to enable Ewing sarcoma oncogenesis and growth, small molecule YK-4-279 disrupts this complex in cells
physiological function
human host DDX21 RNA helicase restricts influenza A virus by binding PB1 protein and inhibiting polymerase assembly, resulting in reduced viral RNA and protein synthesis. Later during infection, the viral NS1 protein overcomes this restriction by binding to DDX21 and displacing PB1. DDX21 binds to a region of the NS1 N-terminal domain that also participates in other critical functions
physiological function
RNA helicase A is a member of DExH-box RNA helicases, and has been reported to promote replication of a number of viruses, such as hepatitis C virus, foot-and mouth disease virus, influenza A virus, and HIV-1. The enzyme regulates a variety of RNA metabolism processes including HIV-1 replication
physiological function
RNA helicase DHX34 use ATP hydrolysis to promote directly or indirectly RNA-RNA unwinding, RNA-protein dissociation, and protein-protein interactions. It activates nonsense-mediated mRNA decay, a surveillance pathway that eliminates mRNAs that contain premature termination codons preventing the synthesis of truncated proteins mechanism, overview. Enzyme DHX34 promotes UPF1 phosphorylation. Role for helicase DHX34 in the active remodeling of the SURF complex promoting its transition to the DECID complex, overview. DHX34-dependent recruitment of UPF2 and eIF4A3 to UPF1 complexes. DHX34 supports the transition from SURF to DECID resulting in UPF1 phosphorylation and release of the eRFs from the PTC resulting in targeting of the faulty mRNA for degradation
physiological function
RNA helicases are involved in many biologically relevant processes, not only as RNA chaperones, but also as signal transducers, scaffolds of molecular complexes, and regulatory elements. Cells require either the presence of controlled chemical environments or the assistance of specialized proteins to ensure the stabilization and proper RNA folding. RNA chaperones or RNA helicases help RNA to reach and maintain its functional conformational state. Some of these RNA helicases are chaperone-like proteins that prevent RNA to reach energy minima characterized by an incorrect conformational state during folding. Others are correctors of misfolded RNAs, able to resolve incorrect structural elements and to produce single stranded RNA
physiological function
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RNA helicases are involved in many biologically relevant processes, not only as RNA chaperones, but also as signal transducers, scaffolds of molecular complexes, and regulatory elements. Cells require either the presence of controlled chemical environments or the assistance of specialized proteins to ensure the stabilization and proper RNA folding. RNA chaperones or RNA helicases help RNA to reach and maintain its functional conformational state. Some of these RNA helicases are chaperone-like proteins that prevent RNA to reach energy minima characterized by an incorrect conformational state during folding. Others are correctors of misfolded RNAs, able to resolve incorrect structural elements and to produce single stranded RNA
physiological function
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RNA helicases are involved in many biologically relevant processes, not only as RNA chaperones, but also as signal transducers, scaffolds of molecular complexes, and regulatory elements. Cells require either the presence of controlled chemical environments or the assistance of specialized proteins to ensure the stabilization and proper RNA folding. RNA chaperones or RNA helicases help RNA to reach and maintain its functional conformational state. Some of these RNA helicases are chaperone-like proteins that prevent RNA to reach energy minima characterized by an incorrect conformational state during folding. Others are correctors of misfolded RNAs, able to resolve incorrect structural elements and to produce single stranded RNA
physiological function
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RNA helicases are involved in many biologically relevant processes, not only as RNA chaperones, but also as signal transducers, scaffolds of molecular complexes, and regulatory elements. Cells require either the presence of controlled chemical environments or the assistance of specialized proteins to ensure the stabilization and proper RNA folding. RNA chaperones or RNA helicases help RNA to reach and maintain its functional conformational state. Some of these RNA helicases are chaperone-like proteins that prevent RNA to reach energy minima characterized by an incorrect conformational state during folding. Others are correctors of misfolded RNAs, able to resolve incorrect structural elements and to produce single stranded RNA
physiological function
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RNA helicases are involved in many biologically relevant processes, not only as RNA chaperones, but also as signal transducers, scaffolds of molecular complexes, and regulatory elements. Cells require either the presence of controlled chemical environments or the assistance of specialized proteins to ensure the stabilization and proper RNA folding. RNA chaperones or RNA helicases help RNA to reach and maintain its functional conformational state. Some of these RNA helicases are chaperone-like proteins that prevent RNA to reach energy minima characterized by an incorrect conformational state during folding. Others are correctors of misfolded RNAs, able to resolve incorrect structural elements and to produce single stranded RNA
physiological function
RNA helicases are involved in many biologically relevant processes, not only as RNA chaperones, but also as signal transducers, scaffolds of molecular complexes, and regulatory elements. Cells require either the presence of controlled chemical environments or the assistance of specialized proteins to ensure the stabilization and proper RNA folding. RNA chaperones or RNA helicases help RNA to reach and maintain its functional conformational state. Some of these RNA helicases are chaperone-like proteins that prevent RNA to reach energy minima characterized by an incorrect conformational state during folding. Others are correctors of misfolded RNAs, able to resolve incorrect structural elements and to produce single stranded RNA
physiological function
RNA helicases are involved in many biologically relevant processes, not only as RNA chaperones, but also as signal transducers, scaffolds of molecular complexes, and regulatory elements. Cells require either the presence of controlled chemical environments or the assistance of specialized proteins to ensure the stabilization and proper RNA folding. RNA chaperones or RNA helicases help RNA to reach and maintain its functional conformational state. Some of these RNA helicases are chaperone-like proteins that prevent RNA to reach energy minima characterized by an incorrect conformational state during folding. Others are correctors of misfolded RNAs, able to resolve incorrect structural elements and to produce single stranded RNA
physiological function
RNA helicases are involved in many biologically relevant processes, not only as RNA chaperones, but also as signal transducers, scaffolds of molecular complexes, and regulatory elements. Cells require either the presence of controlled chemical environments or the assistance of specialized proteins to ensure the stabilization and proper RNA folding. RNA chaperones or RNA helicases help RNA to reach and maintain its functional conformational state. Some of these RNA helicases are chaperone-like proteins that prevent RNA to reach energy minima characterized by an incorrect conformational state during folding. Others are correctors of misfolded RNAs, able to resolve incorrect structural elements and to produce single stranded RNA
physiological function
RNA helicases are involved in many biologically relevant processes, not only as RNA chaperones, but also as signal transducers, scaffolds of molecular complexes, and regulatory elements. Cells require either the presence of controlled chemical environments or the assistance of specialized proteins to ensure the stabilization and proper RNA folding. RNA chaperones or RNA helicases help RNA to reach and maintain its functional conformational state. Some of these RNA helicases are chaperone-like proteins that prevent RNA to reach energy minima characterized by an incorrect conformational state during folding. Others are correctors of misfolded RNAs, able to resolve incorrect structural elements and to produce single stranded RNA. In higher eukaryotes, the RNA helicase family has also evolved to perform more specific tasks often comprising heterogeneous interaction partners that are tethered to specific RNA locations. RNA helicases are RNA-binding proteins able to resolve secondary and tertiary RNA structures in an active manner, in some cases coupling this enzymatic activity to the hydrolysis of ATP. RNA helicases involved in viral infections, overview
physiological function
RNA helicases regulate the biogenesis and homeostasis of RNA, functional significance of RNA helicases in aging, a large fraction of RNA helicases regulate the lifespan of Caenorhabditis elegans. Enzyme Hel-1 promotes longevity by specifically activating the DAF-16/forkhead box O (FOXO) transcription factor signaling pathway. HEL-1 is required for the longevity conferred by reduced insulin/insulin-like growth factor 1 signaling and is sufficient for extending lifespan. The expression of HEL-1 in the intestine and neurons contributes to longevity. HEL-1 enhances the induction of a large fraction of DAF-16 target genes
physiological function
the balance between stem cell maintenance and neuronal differentiation depends on cell-fate determinants such as TRIM32. TRIM32 associates with the RNA-induced silencing complex and increases the activity of microRNAs such as Let-7a. The RNA helicase DDX6 is involved in microRNA regulation. Helicase DDX6 colocalizes with TRIM32 in neural stem cells and neurons and increases the activity of Let-7a. Enzyme DDX6 is necessary and sufficient for neuronal differentiation and it functions in cooperation with TRIM32
physiological function
the enzyme is under strong developmental control, and its abundance sharply peaks in the sink-source transition zone of developing maize leaves, coincident with the plastid biogenesis machinery
physiological function
the enzyme is under strong developmental control. Cross talk between the chloroplast and the nucleus is used to regulate RH3 levels. Enzyme RH3 functions in the splicing of group II introns and possibly also contributes to the assembly of the 50S ribosomal particle
physiological function
the Listeria RNA helicase Lmo1722 is essential for growth at low temperatures, motility, and rRNA processing and is important for ribosomal maturation, being associated mainly with the 50S subunit of the ribosome. RNA helicase Lmo1722 is required for optimal growth at low temperatures, whereas it is dispensable at 37°C. The C-terminal part of enzyme Lmo1722 is redundant for low-temperature growth, motility, 23S rRNA processing, and appropriate ribosomal maturation, but the C-terminus is important for proper guidance of Lmo1722 to the 50S subunit
physiological function
Upf1 is a RNA helicase essential for nonsense-mediated mRNA decay, Upf1 is an efficient ribonucleoprotein complex remodeler. Upf1, once recruited onto nonsense-mediated mRNA decay targets, can scan the entire transcript to irreversibly remodel the mRNP, facilitating its degradation by the nonsense-mediated mRNA decay machinery. The ATPase activity of Upf1 is required for the correct progression of nonsense-mediated mRNA decay, a quality-control mechanism that eliminates mRNAs containing premature translation termination codons and also regulates the expression of numerous mRNAs carrying nonsense-mediated mRNA decay target features. The enzyme is specifically recruited to specific targets by an intricate stepwise and translation-dependent pathway
physiological function
analysis of a distinct mechanism of regulation of RNA helicases, wherein alternative splicing leads to subtle structural rearrangements within the protein that are critical to modulate enzyme movements and catalytic activity
physiological function
Brr2 is an essential component of spliceosome. Brr2 catalyzes an ATP-dependent unwinding of the U4/U6 RNA duplex, which is a critical step for spliceosomal activation
physiological function
CshA is required for efficient turnover of the bulk of mRNAs. For efficient degradation, the RNA helicase interacts through its C-terminal extension with the degradosome components. The molecular function of the RNA helicase might be the destabilisation of secondary structures or the removal of hindering RNA binding proteins
physiological function
CshA likely stabilizes selective mRNAs and sRNAs in vivo and as a result enhances Staphylococcus aureus survival upon MazFsa induction during stress
physiological function
CshA likely stabilizes selective mRNAs and sRNAs in vivo and as a result enhances Staphylococcus aureus survival upon MazFsa induction during stress. CshA protects sarA mRNA but not spa mRNA in vivo. The enzyme is a DEAD box RNA helicase, an enzyme with distinct helicase and ATPase domains that unwinds double-stranded RNA in an ATP-dependent manner and possesses ATPase activity
physiological function
DbpA is a DEAD-box RNA helicase implicated in RNA structural rearrangements in the peptidyl transferase center. DbpA performs RNA structural isomerizations in a region of the ribosome that is evolutionarily conserved in all organisms and crucial for their survival
physiological function
Ddx27 plays a pivotal role in skeletal muscle regeneration
physiological function
Ded1 is a DEAD-box RNA helicase with essential roles in translation initiation. It binds to the eukaryotic initiation factor 4F (eIF4F) complex and promotes 48S preinitiation complex assembly and start-site scanning of 5' untranslated regions of mRNAs. Role of the enzyme in the translational response during target of rapamycin (TOR)C1 inhibition and function of Ded1 as a translation repressor, overview. Both the rapamycin resistance and impaired survivability following nutrient starvation suggest an important role for the Ded1 C-terminus in the cellular changes that occur during long-term nutrient stress and inhibition of TORC1. Ded1 enzymatic activity and interaction with eIF4G1 are required, while homooligomerization may be dispensable, mapping of the functional requirements for Ded1 in the translaxadtional response. Ded1 stalls translation and specifically removes eIF4G1 from translation preinitiation complexes, thus removing eIF4G1 from the translating mRNA pool and leading to the codegradation of both proteins. The enzyme's role is conserved and may be implicated in pathologies such as oncogenesis
physiological function
enzyme CshA is a component of the RNA degradosome and plays important roles in RNA turnover
physiological function
enzyme DeaD stimulates ExsA synthesis at the posttranscriptional level, DeaD promotes T3SS expression. ExsA is the master regulator of T3SS transcription. The Pseudomonas aeruginosa type III secretion system (T3SS) is a primary virulence factor important for phagocytic avoidance, disruption of host cell signaling, and host cell cytotoxicity. The expression, synthesis, and activity of ExsA is tightly regulated by both intrinsic and extrinsic factors. Intrinsic regulation consists of the ExsECDA partner-switching cascade, while extrinsic factors include global regulators that alter exsA transcription and/or translation. DeaD relaxes mRNA secondary structure to promote exsA translation and altering the mRNA sequence of exsA or the native exsA Shine-Dalgarno sequence relieves the requirement for DeaD in vivo. Regulatory mechanism for DeaD, overview. DeaD promotes ExsA synthesis at a posttranscriptional level by activating ExsA translation. The RNA helicase plays a critical role in promoting ExsA synthesis
physiological function
FRQ-interacting RNA helicase (FRH) is an ATP-dependent RNA helicase that functions in the central transcriptional-translational feedback loop of the Neurospora crassa circadian clock. In the Neurospora crassa circadian clock, a protein complex of frequency (FRQ), casein kinase 1a (CK1a), and the FRQ-interacting RNA helicase (FRH) rhythmically represses gene expression by the white-collar complex (WCC). FRH is essential for cell viability, although FRH helicase activity does not play an essential role in the clock, but rather acts to mediate contacts among FRQ, CK1a and the WCC through interactions involving its N-terminus and KOW module
physiological function
functions and regulation of the Brr2 RNA helicase during splicing, structure-function analysis, overview. Brr2 is transported to the nucleus independent of other U5 snRNP components and its helicase activity may have to be shut off during this phase to avoid detrimental off-target effects. Once assembled in the nucleus, mature U5 snRNP joins the U4/U6 di-snRNP to form the U4/U6-U5 trisnRNP, in which Brr2 already encounters its U4/U6 di-snRNA substrate before incorporation into the spliceosome. Brr2 requires tight regulation. Isolated Brr2 is a comparatively weak helicase and its U4/U6 di-snRNA substrate is stabilized by extensive base pairing and bound proteins, suggesting that the helicase may also depend on specific activation to efficiently unwind the U4/U6 duplex at the right time. Implications for Brr2-dependent proofreading and regulation of alternative splicing, model for putative Brr2-mediated enhancement of splicing fidelity and regulation of alternative splicing. Brr2 may be more or less prone to disrupt the tri-snRNP in a non-productive fashion, thus differentially channeling the different substrates along the splicing or discard pathways. Similarly, depending on the level of Brr2 inhibition in competing alternative splicing scenarios, the helicase may elicit spliceosome activation slowly or quickly, kinetically controlling the levels of protein isoforms produced
physiological function
functions and regulation of the Brr2 RNA helicase during splicing, structure-function analysis, overview. Brr2 is transported to the nucleus independent of other U5 snRNP components and its helicase activity may have to be shut off during this phase to avoid detrimental off-target effects. Once assembled in the nucleus, mature U5 snRNP joins the U4/U6 di-snRNP to form the U4/U6-U5 trisnRNP, in which Brr2 already encounters its U4/U6 di-snRNA substrate before incorporation into the spliceosome. Brr2 requires tight regulation. Isolated Brr2 is a comparatively weak helicase and its U4/U6 di-snRNA substrate is stabilized by extensive base pairing and bound proteins, suggesting that the helicase may also depend on specific activation to efficiently unwind the U4/U6 duplex at the right time. Implications for Brr2-dependent proofreading and regulation of alternative splicing, model for putative Brr2-mediated enhancement of splicing fidelity and regulation of alternative splicing. Brr2 may be more or less prone to disrupt the tri-snRNP in a non-productive fashion, thus differentially channeling the different substrates along the splicing or discard pathways. Similarly, depending on the level of Brr2 inhibition in competing alternative splicing scenarios, the helicase may elicit spliceosome activation slowly or quickly, kinetically controlling the levels of protein isoforms produced
physiological function
increased size exclusion limit2 (ISE2) is a chloroplast-localized RNA helicase that is indispensable for proper plant development. Enzyme ISE2 is required for multiple chloroplast RNA processing steps in Arabidopsis thaliana. ISE2 is required for the splicing of group II introns from chloroplast transcripts. ISE2 is required for site-specific chloroplast C-to-U RNA editing. ISE2 is required for chloroplast rRNA processing and splicing of group II introns. And ISE2 is required for accumulation of 30S and 50S ribosomal RNAs and chloroplast-encoded proteins
physiological function
p68 is necessary for cell growth and participates in the early development and maturation of some organs. Interestingly, p68 is a transcriptional coactivator of numerous oncogenic transcription factors, including nuclear factor-kappabeta (NF-kappabeta), estrogen receptor alpha (ERalpha), beta-catenin, androgen receptor, Notch transcriptional activation complex, p53 and signal transducer, and activator of transcription 3 (STAT3). Role of p68 (DDX5) in multiple dysregulated cellular processes in various cancers and its abnormal expression indicate the importance of this factor in tumor development, overview. The role of p68 in cancer is complex and depends on the cellular microenvironment and interacting factors. Translocation of p68 to the promoters of tumor-promoting factors, such as cyclin D1 and c-Myc, and their activation converts them to transcription initiator. P68 as a coactivator of AF1 induces the proliferation of breast cancer cells. p68 modulates the expression of target genes in part through interaction with long noncoding RNAs. P68 exhibits a close relation with TCF4-beta-catenin in the MCF7, MDA-MB 231, and 4T1 breast cancer cell lines. P68 is a coactivator of p53 and modulates the p53 DNA damage response in breast cancer cell line MCF-7. Various breast cancer cell lines exhibit different dependence on DDX5 expression. P68 can manage cell cycle progression in cancer cell. P68 is also involved in the development of neural or mesodermal tissues, and needed for growth regulation
physiological function
RNA helicase A (RHA) is involved in virtually all aspects of RNA metabolism. It exhibits robust RNA helicase activity in vitro
physiological function
RNA helicase Aquarius is crucial for the assembly of box C and box D (box C/D) small nucleolar RNPs (snoRNPs), whose small nucleolar RNAs (snoRNAs) are found in introns about 50 nt upstream of the BS, i.e., 10 nt upstream of Aquarius's binding site. The ATP hydrolysis by Aquarius is required for efficient pre-mRNA splicing
physiological function
RNA helicase BELLE is involved in circadian rhythmicity and in transposons regulation in Drosophila melanogaster, belle is a putative circadian clock component. BELLE acts as important element in the piRNA-mediated regulation of the transposable elements (TEs) and the specific regulation could represent another level of post-transcriptional control adopted by the clock to ensure the proper rhythmicity. BELLE is implicated in the circadian rhythmicity and in the regulation of endogenous transposable elements (TEs) in both nervous system and gonads
physiological function
RNA helicase Brr2 is implicated in multiple phases of pre-mRNA splicing and thus requires tight regulation. Interplay of cis- and trans-regulatory mechanisms in the spliceosomal RNA helicase Brr2. Brr2 can be autoinhibited via a large N-terminal region folding back onto its helicase core and autoactivated by a catalytically inactive C-terminal helicase cassette. It can be regulated in trans by the Jab1 domain of the Prp8 protein, which can inhibit Brr2 by intermittently inserting a C-terminal tail in the enzyme's RNA-binding tunnel or activate the helicase after removal of this tail. Brr2 autoinhibition can act in concert with Jab1-mediated inhibition. The N-terminal region influences how the Jab1 C-terminal tail interacts at the RNA-binding tunnel. the N-terminal region and the Jab1 C-terminal tail specifically interfere with accommodation of double-stranded and single-stranded regions of an RNA substrate, respectively, mutually reinforcing each other. Regulation based on the N-terminal region requires the presence of the inactive C-terminal helicase cassette, intricate system of regulatory mechanisms, which control Brr2 activities during snRNP assembly and splicing, overview
physiological function
Thermochaetoides thermophila
RNA helicase Brr2 is implicated in multiple phases of pre-mRNA splicing and thus requires tight regulation. Interplay of cis- and trans-regulatory mechanisms in the spliceosomal RNA helicase Brr2. Brr2 can be autoinhibited via a large N-terminal region folding back onto its helicase core and autoactivated by a catalytically inactive C-terminal helicase cassette. It can be regulated in trans by the Jab1 domain of the Prp8 protein, which can inhibit Brr2 by intermittently inserting a C-terminal tail in the enzyme's RNA-binding tunnel or activate the helicase after removal of this tail. Brr2 autoinhibition can act in concert with Jab1-mediated inhibition. The N-terminal region influences how the Jab1 C-terminal tail interacts at the RNA-binding tunnel. the N-terminal region and the Jab1 C-terminal tail specifically interfere with accommodation of double-stranded and single-stranded regions of an RNA substrate, respectively, mutually reinforcing each other. Regulation based on the N-terminal region requires the presence of the inactive C-terminal helicase cassette, intricate system of regulatory mechanisms, which control Brr2 activities during snRNP assembly and splicing, overview
physiological function
RNA helicases DDX5 and DDX17 are multitasking proteins that regulate gene expression in different biological contexts through diverse activities. The enzymes are associated with long noncoding RNAs that are key epigenetic regulators, DDX5 and DDX17 may act through modulating the activity of various ribonucleoprotein complexes that could ensure their targeting to specific chromatin loci. Potential roles of DDX5 and DDX17 in the 3D chromatin organization with impact on gene expression at the transcriptional and post-transcriptional levels
physiological function
RNA helicases DDX5 and DDX17 are multitasking proteins that regulate gene expression in different biological contexts through diverse activities. The enzymes are associated with long noncoding RNAs that are key epigenetic regulators, DDX5 and DDX17 may act through modulating the activity of various ribonucleoprotein complexes that could ensure their targeting to specific chromatin loci. Potential roles of DDX5 and DDX17 in the 3D chromatin organization with impact on gene expression at the transcriptional and post-transcriptional levels. Both RNA helicases are identified as SOX2 binding proteins in glioblastoma cells, suggesting that DDX5 may also be involved in SOX2 transcriptional activity. DDX17 contributes to the activation of SOX2-responsive genes by stabilizing SOX2 binding to its target promoters in ERalpha-positive breast cancer cells. DDX5 and DDX17 directly control the SMAD4-dependent expression of master EMT factors SNAI1 and SNAI2 upon TGF-beta treatment. DDX17 and DDX5 are necessary for repressing the expression of a large subset of neuronal genes in undifferentiated neuroblastoma cells, in cooperation with the REST transcription factor. DDX5 and DDX17 interact and synergize with acetyltransferases CBP (CREB-binding protein) and p300 to activate transcription, such as in the context of SMAD3-mediated transcriptional activation. DDX5 and DDX17 interact with the BRG1 chromatin remodeler. In muscle cells, DDX5 and DDX17 recruit BRG1 to MYOD target genes, increasing the chromatin accessibility for the transcription machinery, which helps coactivate MYOD-dependent transcription
physiological function
RNA helicases DDX5 and DDX17 are multitasking proteins that regulate gene expression in different biological contexts through diverse activities. The enzymes are associated with long noncoding RNAs that are key epigenetic regulators, DDX5 and DDX17 may act through modulating the activity of various ribonucleoprotein complexes that could ensure their targeting to specific chromatin loci. Potential roles of DDX5 and DDX17 in the 3D chromatin organization with impact on gene expression at the transcriptional and post-transcriptional levels. Both RNA helicases are identified as SOX2 binding proteins in glioblastoma cells, suggesting that DDX5 may also be involved in SOX2 transcriptional activity. DDX5 may also contribute to cancer development by modulating various signaling pathways. DDX5 interacts with beta-catenin in non-small-cell lung cancer cells as well as colorectal cancer cells, and it also promotes its nuclear translocation, which is associated with the coactivation of Wnt-responsive genes such as MYC or CCND1. DDX5 and beta-catenin are also involved together in the regulation of androgen receptor (AR) transcriptional activity in prostate cancer cells, where DDX5 promotes the recruitment of both transcription factors to AR target genes. Finally, the interaction between DDX5 and beta-catenin contributes to the epithelial to mesenchymal transition (EMT), a process involved in the formation of metastases. DDX5 has been shown to enhance SMAD3 transcriptional activity in response to TGF-beta. DDX5 and DDX17 directly control the SMAD4-dependent expression of master EMT factors SNAI1 and SNAI2 upon TGF-beta treatment. DDX17 and DDX5 are necessary for repressing the expression of a large subset of neuronal genes in undifferentiated neuroblastoma cells, in cooperation with the REST transcription factor. DDX5 and DDX17 interact and synergize with acetyltransferases CBP (CREB-binding protein) and p300 to activate transcription, such as in the context of SMAD3-mediated transcriptional activation. DDX5 and DDX17 interact with the BRG1 chromatin remodeler. In muscle cells, DDX5 and DDX17 recruit BRG1 to MYOD target genes, increasing the chromatin accessibility for the transcription machinery, which helps coactivate MYOD-dependent transcription. DDX5 may be involved in the control of DNA methylation and/or demethylation of CpG dinucleotides, as it interacts with DNA methyltransferase 3 proteins (DNMT3A and B) as well as with thymine DNA glycosylase (TDG). DDX5 is recruited to chromatin along with both DNMT3A/B and TDG proteins at the beginning of each transcription cycle of an ERalpha-responsive promoter
physiological function
RNA helicases DDX5 and DDX17 are multitasking proteins that regulate gene expression in different biological contexts through diverse activities. The enzymes are associated with long noncoding RNAs that are key epigenetic regulators, DDX5 and DDX17 may act through modulating the activity of various ribonucleoprotein complexes that could ensure their targeting to specific chromatin loci. Potential roles of DDX5 and DDX17 in the 3D chromatin organization with impact on gene expression at the transcriptional and post-transcriptional levels. DDX5 may also contribute to cancer development by modulating various signaling pathways
physiological function
RNA helicases DDX5 and DDX17 are multitasking proteins that regulate gene expression in different biological contexts through diverse activities. The enzymes are associated with long noncoding RNAs that are key epigenetic regulators, DDX5 and DDX17 may act through modulating the activity of various ribonucleoprotein complexes that could ensure their targeting to specific chromatin loci. Potential roles of DDX5 and DDX17 in the 3D chromatin organization with impact on gene expression at the transcriptional and post-transcriptional levels. DDX5 may also contribute to cancer development by modulating various signaling pathways. Murine Ddx5 and Ddx17 are essential for the early stages of myoblast or osteoblast differentiation through their interaction with master transcription factors Myod or Runx2, respectively. In both cases, Ddx5 is recruited to Myod and Runx2 responsive promoters, and it enhances their transcriptional activity. During myogenesis, one consequence is the induced expression of myogenic microRNAs, myogenic transcription factors (Myog or Mef2c), as well as muscle specific genes. DDX17 and DDX5 are necessary for repressing the expression of a large subset of neuronal genes in undifferentiated neuroblastoma cells, in cooperation with the REST transcription factor. DDX5 and DDX17 interact and synergize with acetyltransferases CBP (CREB-binding protein) and p300 to activate transcription, such as in the context of SMAD3-mediated transcriptional activation. DDX5 and DDX17 interact with the BRG1 chromatin remodeler. In muscle cells, DDX5 and DDX17 recruit BRG1 to MYOD target genes, increasing the chromatin accessibility for the transcription machinery, which helps coactivate MYOD-dependent transcription. DDX5 may be involved in the control of DNA methylation and/or demethylation of CpG dinucleotides, as it interacts with DNA methyltransferase 3 proteins (DNMT3A and B) as well as with thymine DNA glycosylase (TDG). DDX5 is recruited to chromatin along with both DNMT3A/B and TDG proteins at the beginning of each transcription cycle of an ERalpha-responsive promoter. During myogenic differentiation of mouse C2C12 cells, both RNA helicases and steroid nuclear receptor activator RNA (SRA)coactivate the transcription factor MyoD, and the joint overexpression of SRA and Ddx5 stimulates the MyoD-induced conversion of mouse embryonic fibroblasts in skeletal muscle cells. The SRA lncRNA can act as a multimodal scaffold for several complexes, and it can be dynamically regulated by RNA helicases
physiological function
RNA helicases DDX5 and DDX17 are multitasking proteins that regulate gene expression in different biological contexts through diverse activities. The enzymes are associated with long noncoding RNAs that are key epigenetic regulators, DDX5 and DDX17 may act through modulating the activity of various ribonucleoprotein complexes that could ensure their targeting to specific chromatin loci. Potential roles of DDX5 and DDX17 in the 3D chromatin organization with impact on gene expression at the transcriptional and post-transcriptional levels. Murine Ddx5 and Ddx17 are essential for the early stages of myoblast or osteoblast differentiation through their interaction with master transcription factors Myod or Runx2, respectively. In both cases, Ddx5 is recruited to Myod and Runx2 responsive promoters, and it enhances their transcriptional activity. During myogenesis, one consequence is the induced expression of myogenic microRNAs, myogenic transcription factors (Myog or Mef2c), as well as muscle specific genes. DDX17 and DDX5 are necessary for repressing the expression of a large subset of neuronal genes in undifferentiated neuroblastoma cells, in cooperation with the REST transcription factor. DDX5 and DDX17 interact and synergize with acetyltransferases CBP (CREB-binding protein) and p300 to activate transcription, such as in the context of SMAD3-mediated transcriptional activation. DDX5 and DDX17 interact with the BRG1 chromatin remodeler. In muscle cells, DDX5 and DDX17 recruit BRG1 to MYOD target genes, increasing the chromatin accessibility for the transcription machinery, which helps coactivate MYOD-dependent transcription. During myogenic differentiation of mouse C2C12 cells, both RNA helicases and steroid nuclear receptor activator RNA (SRA) coactivate the transcription factor MyoD, and the joint overexpression of SRA and Ddx5 stimulates the MyoD-induced conversion of mouse embryonic fibroblasts in skeletal muscle cells. The SRA lncRNA can act as a multimodal scaffold for several complexes, and it can be dynamically regulated by RNA helicases
physiological function
rRNA genes undergo chromatin changes during mouse embryonic stem cell (ESC) differentiation. The establishment of heterochromatin at rRNA genes depends on the processing of IGS-rRNA into pRNA. The RNA helicase DHX9 is a regulator of pRNA processing. DHX9 binds to rRNA genes only upon ESC differentiation and its activity guides TIP5 to rRNA genes and establishes heterochromatin. The production of mature pRNA is essential since it guides the repressor TIP5 to rRNA genes. The processing of IGS-rRNA into pRNA is impaired in embryonic stem cells (ESCs) and activated only upon differentiation. IGS-rRNA abolishes the process of guiding of repressor TIP5 to rRNA genes. The RNA helicase DHX9 associates with IGS-rRNA and TIP5. DHX9 is required for the formation of heterochromatin at rRNA genes through processing of IGS-rRNA into pRNA. DHX9 requires the association of TIP5 with mature pRNA to bind to rRNA genes
physiological function
splicing is catalysed by the spliceosome, a large and dynamic protein-RNA complex consisting of five small nuclear ribonucleoproteins (snRNPs) and, in humans, about 200 accessory proteins. DHX8 is a crucial DEAH-box RNA helicase involved in splicing and required for the release of mature mRNA from the spliceosome. The DEAH/RHA RNA helicase DHX8 is required for the release of mature mRNA from the spliceosome
physiological function
the cold-inducible DEAD-Box RNA helicase AtRH7 regulates plant growth and development under low temperature in Arabidopsis thaliana. AtRH7 affects rRNA biogenesis and is an interactor of Arabidopsis cold shock domain protein 3 (AtCSP3), which is an RNA chaperone involved in cold adaptation. The enzyme can complement the Escherichia coli DELTAcsdA mutant, which is deficient in growth at low temperatures
physiological function
Thermochaetoides thermophila
the DEAH-box helicase Prp43 is a key player in pre-mRNA splicing as well as the maturation of rRNAs, RNA loading mechanism of Prp43, detailed overview. Prp43 acts at the latest stage of the splicing cycle and it is required to dismantle the intron-lariat spliceosome into the excised lariat and the U2-U5-U6 snRNPs. The target substrate of Prp43 during this process is the RNA network between the U2 snRNP and the branch site of the intron. In the spliceosome, Prp43 is crosslinked exclusively to the pre-mRNA and not to any snRNAs. The opening of the tunnel by the displacement of the C-terminal domains is crucial for the helicase function of Prp43
physiological function
the RNA helicase DDX3X is an essential mediator of innate antimicrobial immunity, essential contribution of a non-RLR DExD/H RNA helicase to innate immunity. Enzyme DDX3 is an interactor of the S/T kinase TBK1 which regulates the production of type I Interferons (IFN-I), contributions of DDX3X to hematopoiesis. DDX3X is critically involved in enhancing the expression of numerous antimicrobial genes. DDX3X may contribute to sex differences in immunity to pathogens and inflammatory disease. Besides its role in the regulation of the TBK1-IRF3 axis, DDX3X controls the NFkappaB signaling pathway and has a profound impact on inflammatory cytokine production. DDX3Y, either alone or together with additional Y-chromosomal genes, partially compensates for the loss of the Ddx3x gene, as homozygous female cells and mice show more severe loss-of-function phenotypes
physiological function
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enzyme DeaD stimulates ExsA synthesis at the posttranscriptional level, DeaD promotes T3SS expression. ExsA is the master regulator of T3SS transcription. The Pseudomonas aeruginosa type III secretion system (T3SS) is a primary virulence factor important for phagocytic avoidance, disruption of host cell signaling, and host cell cytotoxicity. The expression, synthesis, and activity of ExsA is tightly regulated by both intrinsic and extrinsic factors. Intrinsic regulation consists of the ExsECDA partner-switching cascade, while extrinsic factors include global regulators that alter exsA transcription and/or translation. DeaD relaxes mRNA secondary structure to promote exsA translation and altering the mRNA sequence of exsA or the native exsA Shine-Dalgarno sequence relieves the requirement for DeaD in vivo. Regulatory mechanism for DeaD, overview. DeaD promotes ExsA synthesis at a posttranscriptional level by activating ExsA translation. The RNA helicase plays a critical role in promoting ExsA synthesis
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physiological function
Thermochaetoides thermophila IMI 039719
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the DEAH-box helicase Prp43 is a key player in pre-mRNA splicing as well as the maturation of rRNAs, RNA loading mechanism of Prp43, detailed overview. Prp43 acts at the latest stage of the splicing cycle and it is required to dismantle the intron-lariat spliceosome into the excised lariat and the U2-U5-U6 snRNPs. The target substrate of Prp43 during this process is the RNA network between the U2 snRNP and the branch site of the intron. In the spliceosome, Prp43 is crosslinked exclusively to the pre-mRNA and not to any snRNAs. The opening of the tunnel by the displacement of the C-terminal domains is crucial for the helicase function of Prp43
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physiological function
Thermochaetoides thermophila IMI 039719
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RNA helicase Brr2 is implicated in multiple phases of pre-mRNA splicing and thus requires tight regulation. Interplay of cis- and trans-regulatory mechanisms in the spliceosomal RNA helicase Brr2. Brr2 can be autoinhibited via a large N-terminal region folding back onto its helicase core and autoactivated by a catalytically inactive C-terminal helicase cassette. It can be regulated in trans by the Jab1 domain of the Prp8 protein, which can inhibit Brr2 by intermittently inserting a C-terminal tail in the enzyme's RNA-binding tunnel or activate the helicase after removal of this tail. Brr2 autoinhibition can act in concert with Jab1-mediated inhibition. The N-terminal region influences how the Jab1 C-terminal tail interacts at the RNA-binding tunnel. the N-terminal region and the Jab1 C-terminal tail specifically interfere with accommodation of double-stranded and single-stranded regions of an RNA substrate, respectively, mutually reinforcing each other. Regulation based on the N-terminal region requires the presence of the inactive C-terminal helicase cassette, intricate system of regulatory mechanisms, which control Brr2 activities during snRNP assembly and splicing, overview
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physiological function
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CshA is required for efficient turnover of the bulk of mRNAs. For efficient degradation, the RNA helicase interacts through its C-terminal extension with the degradosome components. The molecular function of the RNA helicase might be the destabilisation of secondary structures or the removal of hindering RNA binding proteins
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physiological function
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CshA likely stabilizes selective mRNAs and sRNAs in vivo and as a result enhances Staphylococcus aureus survival upon MazFsa induction during stress. CshA protects sarA mRNA but not spa mRNA in vivo. The enzyme is a DEAD box RNA helicase, an enzyme with distinct helicase and ATPase domains that unwinds double-stranded RNA in an ATP-dependent manner and possesses ATPase activity
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physiological function
Thermochaetoides thermophila DSM 1495
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the DEAH-box helicase Prp43 is a key player in pre-mRNA splicing as well as the maturation of rRNAs, RNA loading mechanism of Prp43, detailed overview. Prp43 acts at the latest stage of the splicing cycle and it is required to dismantle the intron-lariat spliceosome into the excised lariat and the U2-U5-U6 snRNPs. The target substrate of Prp43 during this process is the RNA network between the U2 snRNP and the branch site of the intron. In the spliceosome, Prp43 is crosslinked exclusively to the pre-mRNA and not to any snRNAs. The opening of the tunnel by the displacement of the C-terminal domains is crucial for the helicase function of Prp43
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physiological function
Thermochaetoides thermophila DSM 1495
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RNA helicase Brr2 is implicated in multiple phases of pre-mRNA splicing and thus requires tight regulation. Interplay of cis- and trans-regulatory mechanisms in the spliceosomal RNA helicase Brr2. Brr2 can be autoinhibited via a large N-terminal region folding back onto its helicase core and autoactivated by a catalytically inactive C-terminal helicase cassette. It can be regulated in trans by the Jab1 domain of the Prp8 protein, which can inhibit Brr2 by intermittently inserting a C-terminal tail in the enzyme's RNA-binding tunnel or activate the helicase after removal of this tail. Brr2 autoinhibition can act in concert with Jab1-mediated inhibition. The N-terminal region influences how the Jab1 C-terminal tail interacts at the RNA-binding tunnel. the N-terminal region and the Jab1 C-terminal tail specifically interfere with accommodation of double-stranded and single-stranded regions of an RNA substrate, respectively, mutually reinforcing each other. Regulation based on the N-terminal region requires the presence of the inactive C-terminal helicase cassette, intricate system of regulatory mechanisms, which control Brr2 activities during snRNP assembly and splicing, overview
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physiological function
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enzyme DeaD stimulates ExsA synthesis at the posttranscriptional level, DeaD promotes T3SS expression. ExsA is the master regulator of T3SS transcription. The Pseudomonas aeruginosa type III secretion system (T3SS) is a primary virulence factor important for phagocytic avoidance, disruption of host cell signaling, and host cell cytotoxicity. The expression, synthesis, and activity of ExsA is tightly regulated by both intrinsic and extrinsic factors. Intrinsic regulation consists of the ExsECDA partner-switching cascade, while extrinsic factors include global regulators that alter exsA transcription and/or translation. DeaD relaxes mRNA secondary structure to promote exsA translation and altering the mRNA sequence of exsA or the native exsA Shine-Dalgarno sequence relieves the requirement for DeaD in vivo. Regulatory mechanism for DeaD, overview. DeaD promotes ExsA synthesis at a posttranscriptional level by activating ExsA translation. The RNA helicase plays a critical role in promoting ExsA synthesis
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physiological function
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CshA likely stabilizes selective mRNAs and sRNAs in vivo and as a result enhances Staphylococcus aureus survival upon MazFsa induction during stress
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physiological function
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enzyme DeaD stimulates ExsA synthesis at the posttranscriptional level, DeaD promotes T3SS expression. ExsA is the master regulator of T3SS transcription. The Pseudomonas aeruginosa type III secretion system (T3SS) is a primary virulence factor important for phagocytic avoidance, disruption of host cell signaling, and host cell cytotoxicity. The expression, synthesis, and activity of ExsA is tightly regulated by both intrinsic and extrinsic factors. Intrinsic regulation consists of the ExsECDA partner-switching cascade, while extrinsic factors include global regulators that alter exsA transcription and/or translation. DeaD relaxes mRNA secondary structure to promote exsA translation and altering the mRNA sequence of exsA or the native exsA Shine-Dalgarno sequence relieves the requirement for DeaD in vivo. Regulatory mechanism for DeaD, overview. DeaD promotes ExsA synthesis at a posttranscriptional level by activating ExsA translation. The RNA helicase plays a critical role in promoting ExsA synthesis
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physiological function
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FRQ-interacting RNA helicase (FRH) is an ATP-dependent RNA helicase that functions in the central transcriptional-translational feedback loop of the Neurospora crassa circadian clock. In the Neurospora crassa circadian clock, a protein complex of frequency (FRQ), casein kinase 1a (CK1a), and the FRQ-interacting RNA helicase (FRH) rhythmically represses gene expression by the white-collar complex (WCC). FRH is essential for cell viability, although FRH helicase activity does not play an essential role in the clock, but rather acts to mediate contacts among FRQ, CK1a and the WCC through interactions involving its N-terminus and KOW module
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physiological function
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enzyme CshA is a component of the RNA degradosome and plays important roles in RNA turnover
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physiological function
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increased size exclusion limit2 (ISE2) is a chloroplast-localized RNA helicase that is indispensable for proper plant development. Enzyme ISE2 is required for multiple chloroplast RNA processing steps in Arabidopsis thaliana. ISE2 is required for the splicing of group II introns from chloroplast transcripts. ISE2 is required for site-specific chloroplast C-to-U RNA editing. ISE2 is required for chloroplast rRNA processing and splicing of group II introns. And ISE2 is required for accumulation of 30S and 50S ribosomal RNAs and chloroplast-encoded proteins
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physiological function
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enzyme DeaD stimulates ExsA synthesis at the posttranscriptional level, DeaD promotes T3SS expression. ExsA is the master regulator of T3SS transcription. The Pseudomonas aeruginosa type III secretion system (T3SS) is a primary virulence factor important for phagocytic avoidance, disruption of host cell signaling, and host cell cytotoxicity. The expression, synthesis, and activity of ExsA is tightly regulated by both intrinsic and extrinsic factors. Intrinsic regulation consists of the ExsECDA partner-switching cascade, while extrinsic factors include global regulators that alter exsA transcription and/or translation. DeaD relaxes mRNA secondary structure to promote exsA translation and altering the mRNA sequence of exsA or the native exsA Shine-Dalgarno sequence relieves the requirement for DeaD in vivo. Regulatory mechanism for DeaD, overview. DeaD promotes ExsA synthesis at a posttranscriptional level by activating ExsA translation. The RNA helicase plays a critical role in promoting ExsA synthesis
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physiological function
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enzyme DeaD stimulates ExsA synthesis at the posttranscriptional level, DeaD promotes T3SS expression. ExsA is the master regulator of T3SS transcription. The Pseudomonas aeruginosa type III secretion system (T3SS) is a primary virulence factor important for phagocytic avoidance, disruption of host cell signaling, and host cell cytotoxicity. The expression, synthesis, and activity of ExsA is tightly regulated by both intrinsic and extrinsic factors. Intrinsic regulation consists of the ExsECDA partner-switching cascade, while extrinsic factors include global regulators that alter exsA transcription and/or translation. DeaD relaxes mRNA secondary structure to promote exsA translation and altering the mRNA sequence of exsA or the native exsA Shine-Dalgarno sequence relieves the requirement for DeaD in vivo. Regulatory mechanism for DeaD, overview. DeaD promotes ExsA synthesis at a posttranscriptional level by activating ExsA translation. The RNA helicase plays a critical role in promoting ExsA synthesis
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physiological function
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enzyme DeaD stimulates ExsA synthesis at the posttranscriptional level, DeaD promotes T3SS expression. ExsA is the master regulator of T3SS transcription. The Pseudomonas aeruginosa type III secretion system (T3SS) is a primary virulence factor important for phagocytic avoidance, disruption of host cell signaling, and host cell cytotoxicity. The expression, synthesis, and activity of ExsA is tightly regulated by both intrinsic and extrinsic factors. Intrinsic regulation consists of the ExsECDA partner-switching cascade, while extrinsic factors include global regulators that alter exsA transcription and/or translation. DeaD relaxes mRNA secondary structure to promote exsA translation and altering the mRNA sequence of exsA or the native exsA Shine-Dalgarno sequence relieves the requirement for DeaD in vivo. Regulatory mechanism for DeaD, overview. DeaD promotes ExsA synthesis at a posttranscriptional level by activating ExsA translation. The RNA helicase plays a critical role in promoting ExsA synthesis
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physiological function
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Ded1 is a DEAD-box RNA helicase with essential roles in translation initiation. It binds to the eukaryotic initiation factor 4F (eIF4F) complex and promotes 48S preinitiation complex assembly and start-site scanning of 5' untranslated regions of mRNAs. Role of the enzyme in the translational response during target of rapamycin (TOR)C1 inhibition and function of Ded1 as a translation repressor, overview. Both the rapamycin resistance and impaired survivability following nutrient starvation suggest an important role for the Ded1 C-terminus in the cellular changes that occur during long-term nutrient stress and inhibition of TORC1. Ded1 enzymatic activity and interaction with eIF4G1 are required, while homooligomerization may be dispensable, mapping of the functional requirements for Ded1 in the translaxadtional response. Ded1 stalls translation and specifically removes eIF4G1 from translation preinitiation complexes, thus removing eIF4G1 from the translating mRNA pool and leading to the codegradation of both proteins. The enzyme's role is conserved and may be implicated in pathologies such as oncogenesis
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physiological function
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functions and regulation of the Brr2 RNA helicase during splicing, structure-function analysis, overview. Brr2 is transported to the nucleus independent of other U5 snRNP components and its helicase activity may have to be shut off during this phase to avoid detrimental off-target effects. Once assembled in the nucleus, mature U5 snRNP joins the U4/U6 di-snRNP to form the U4/U6-U5 trisnRNP, in which Brr2 already encounters its U4/U6 di-snRNA substrate before incorporation into the spliceosome. Brr2 requires tight regulation. Isolated Brr2 is a comparatively weak helicase and its U4/U6 di-snRNA substrate is stabilized by extensive base pairing and bound proteins, suggesting that the helicase may also depend on specific activation to efficiently unwind the U4/U6 duplex at the right time. Implications for Brr2-dependent proofreading and regulation of alternative splicing, model for putative Brr2-mediated enhancement of splicing fidelity and regulation of alternative splicing. Brr2 may be more or less prone to disrupt the tri-snRNP in a non-productive fashion, thus differentially channeling the different substrates along the splicing or discard pathways. Similarly, depending on the level of Brr2 inhibition in competing alternative splicing scenarios, the helicase may elicit spliceosome activation slowly or quickly, kinetically controlling the levels of protein isoforms produced
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physiological function
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FRQ-interacting RNA helicase (FRH) is an ATP-dependent RNA helicase that functions in the central transcriptional-translational feedback loop of the Neurospora crassa circadian clock. In the Neurospora crassa circadian clock, a protein complex of frequency (FRQ), casein kinase 1a (CK1a), and the FRQ-interacting RNA helicase (FRH) rhythmically represses gene expression by the white-collar complex (WCC). FRH is essential for cell viability, although FRH helicase activity does not play an essential role in the clock, but rather acts to mediate contacts among FRQ, CK1a and the WCC through interactions involving its N-terminus and KOW module
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physiological function
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FRQ-interacting RNA helicase (FRH) is an ATP-dependent RNA helicase that functions in the central transcriptional-translational feedback loop of the Neurospora crassa circadian clock. In the Neurospora crassa circadian clock, a protein complex of frequency (FRQ), casein kinase 1a (CK1a), and the FRQ-interacting RNA helicase (FRH) rhythmically represses gene expression by the white-collar complex (WCC). FRH is essential for cell viability, although FRH helicase activity does not play an essential role in the clock, but rather acts to mediate contacts among FRQ, CK1a and the WCC through interactions involving its N-terminus and KOW module
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physiological function
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FRQ-interacting RNA helicase (FRH) is an ATP-dependent RNA helicase that functions in the central transcriptional-translational feedback loop of the Neurospora crassa circadian clock. In the Neurospora crassa circadian clock, a protein complex of frequency (FRQ), casein kinase 1a (CK1a), and the FRQ-interacting RNA helicase (FRH) rhythmically represses gene expression by the white-collar complex (WCC). FRH is essential for cell viability, although FRH helicase activity does not play an essential role in the clock, but rather acts to mediate contacts among FRQ, CK1a and the WCC through interactions involving its N-terminus and KOW module
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physiological function
Thermochaetoides thermophila CBS 144.50
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the DEAH-box helicase Prp43 is a key player in pre-mRNA splicing as well as the maturation of rRNAs, RNA loading mechanism of Prp43, detailed overview. Prp43 acts at the latest stage of the splicing cycle and it is required to dismantle the intron-lariat spliceosome into the excised lariat and the U2-U5-U6 snRNPs. The target substrate of Prp43 during this process is the RNA network between the U2 snRNP and the branch site of the intron. In the spliceosome, Prp43 is crosslinked exclusively to the pre-mRNA and not to any snRNAs. The opening of the tunnel by the displacement of the C-terminal domains is crucial for the helicase function of Prp43
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physiological function
Thermochaetoides thermophila CBS 144.50
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RNA helicase Brr2 is implicated in multiple phases of pre-mRNA splicing and thus requires tight regulation. Interplay of cis- and trans-regulatory mechanisms in the spliceosomal RNA helicase Brr2. Brr2 can be autoinhibited via a large N-terminal region folding back onto its helicase core and autoactivated by a catalytically inactive C-terminal helicase cassette. It can be regulated in trans by the Jab1 domain of the Prp8 protein, which can inhibit Brr2 by intermittently inserting a C-terminal tail in the enzyme's RNA-binding tunnel or activate the helicase after removal of this tail. Brr2 autoinhibition can act in concert with Jab1-mediated inhibition. The N-terminal region influences how the Jab1 C-terminal tail interacts at the RNA-binding tunnel. the N-terminal region and the Jab1 C-terminal tail specifically interfere with accommodation of double-stranded and single-stranded regions of an RNA substrate, respectively, mutually reinforcing each other. Regulation based on the N-terminal region requires the presence of the inactive C-terminal helicase cassette, intricate system of regulatory mechanisms, which control Brr2 activities during snRNP assembly and splicing, overview
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physiological function
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the Listeria RNA helicase Lmo1722 is essential for growth at low temperatures, motility, and rRNA processing and is important for ribosomal maturation, being associated mainly with the 50S subunit of the ribosome. RNA helicase Lmo1722 is required for optimal growth at low temperatures, whereas it is dispensable at 37°C. The C-terminal part of enzyme Lmo1722 is redundant for low-temperature growth, motility, 23S rRNA processing, and appropriate ribosomal maturation, but the C-terminus is important for proper guidance of Lmo1722 to the 50S subunit
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physiological function
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enzyme CshA is a component of the RNA degradosome and plays important roles in RNA turnover
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physiological function
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enzyme DeaD stimulates ExsA synthesis at the posttranscriptional level, DeaD promotes T3SS expression. ExsA is the master regulator of T3SS transcription. The Pseudomonas aeruginosa type III secretion system (T3SS) is a primary virulence factor important for phagocytic avoidance, disruption of host cell signaling, and host cell cytotoxicity. The expression, synthesis, and activity of ExsA is tightly regulated by both intrinsic and extrinsic factors. Intrinsic regulation consists of the ExsECDA partner-switching cascade, while extrinsic factors include global regulators that alter exsA transcription and/or translation. DeaD relaxes mRNA secondary structure to promote exsA translation and altering the mRNA sequence of exsA or the native exsA Shine-Dalgarno sequence relieves the requirement for DeaD in vivo. Regulatory mechanism for DeaD, overview. DeaD promotes ExsA synthesis at a posttranscriptional level by activating ExsA translation. The RNA helicase plays a critical role in promoting ExsA synthesis
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physiological function
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FRQ-interacting RNA helicase (FRH) is an ATP-dependent RNA helicase that functions in the central transcriptional-translational feedback loop of the Neurospora crassa circadian clock. In the Neurospora crassa circadian clock, a protein complex of frequency (FRQ), casein kinase 1a (CK1a), and the FRQ-interacting RNA helicase (FRH) rhythmically represses gene expression by the white-collar complex (WCC). FRH is essential for cell viability, although FRH helicase activity does not play an essential role in the clock, but rather acts to mediate contacts among FRQ, CK1a and the WCC through interactions involving its N-terminus and KOW module
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additional information
domain organization of RH3 protein
additional information
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domain organization of RH3 protein
additional information
domain organization of RH3 protein. RH3 and ClpR2 interact genetically, but RH3 is unlikely to be a substrate for the Clp protease
additional information
influenza A virus likely uses the DDX21-NS1 interaction not only to overcome restriction but also to regulate the viral life cycle
additional information
modeling of the late phases of nonsense-mediated mRNA decay
additional information
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modeling of the late phases of nonsense-mediated mRNA decay
additional information
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molecular mechanism of dsRNA unwinding by yeast Mss116p helicase, overview
additional information
molecular mechanism of dsRNA unwinding by yeast Mss116p helicase, overview
additional information
molecular mechanism of dsRNA unwinding by yeast Mss116p helicase, overview
additional information
RNA helicase A contains two double-stranded RNA binding domains (dsRBD1 and dsRBD2) at the N-terminus. Each dsRBD contains two invariant lysine residues critical for the binding of isolated dsRBDs to RNA. The conserved lysine residues of dsRBDs play critical roles in the promotion of HIV-1 production by RNA helicase A
additional information
a conserved structural element in the RNA helicase UPF1 regulates its catalytic activity in an isoform-specific manner. UPF1 molecular mechanisms, catalytic activity and regulation, overview. The regulatory loop in isoform 1 (UPF1_1) is 11 residues longer than that of isoform 2 (UPF1_2). This small insertion in UPF11 leads to a 2fold increase in its translocation and ATPase activities. Structure analysis and comparisons of wild-type and mutant forms of the two isozymes, detailed overview
additional information
DHX8 is composed of a highly variable N-terminal domain, and a conserved C-terminal helicase domain. The latter contains two RecA domains, RecA1 and RecA2, that form the helicase core and contain up to 12 characteristic motifs that participate in ATP binding and hydrolysis, RNA binding and helicase activity. In addition to the RecA domains, the DHX8 helicase domain contains C-terminally located winged-helix (WH), ratchet-like and oligonucleotide binding (OB)-fold domains. RNA-bound DHX8DELTA547-A6 structure represents a state in the RNA translocation mechanism immediately following ADP release and shows extensive flexibility in the conserved DEAH motif and P-loop, which may facilitate nucleotide release. Compared with other helicase structures, DHX8DELTA547-A6 reveals unexpected differences in the interactions between the RNA substrate and the DEAH-specific hook-turn motif
additional information
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DHX8 is composed of a highly variable N-terminal domain, and a conserved C-terminal helicase domain. The latter contains two RecA domains, RecA1 and RecA2, that form the helicase core and contain up to 12 characteristic motifs that participate in ATP binding and hydrolysis, RNA binding and helicase activity. In addition to the RecA domains, the DHX8 helicase domain contains C-terminally located winged-helix (WH), ratchet-like and oligonucleotide binding (OB)-fold domains. RNA-bound DHX8DELTA547-A6 structure represents a state in the RNA translocation mechanism immediately following ADP release and shows extensive flexibility in the conserved DEAH motif and P-loop, which may facilitate nucleotide release. Compared with other helicase structures, DHX8DELTA547-A6 reveals unexpected differences in the interactions between the RNA substrate and the DEAH-specific hook-turn motif
additional information
DHX9 is characterized by two copies of a double-stranded RNA binding domain (DSRM) at the N-terminus, a helicase core domain (HrpA) in the central region, and an RGG-rich region at the carboxyl terminus, which confers both RNA and DNA helicase activities
additional information
mutational analysis shows that only the C-terminus of the RNA helicase CshA, representing the highly variable region of the molecule, is necessary for binding to sarA mRNA
additional information
mutational analysis shows that only the C-terminus of the RNA helicase CshA, representing the highly variable region of the molecule, is necessary for binding to sarA mRNA
additional information
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mutational analysis shows that only the C-terminus of the RNA helicase CshA, representing the highly variable region of the molecule, is necessary for binding to sarA mRNA
additional information
Thermochaetoides thermophila
RNA loading mechanism of Prp43, overview. Prp43 binds RNA in a sequence-independent fashion. Analysis of crystal structures of Prp43 complexes in different functional states and the analysis of structure-based mutants providing insights into the unwinding and loading mechanism of RNAs. The Prp43-ATP-analogue-RNA complex shows the localization of the RNA inside a tunnel formed by the two RecA-like and C-terminal domains. In the ATP-bound state this tunnel can be transformed into a groove prone for RNA binding by large rearrangements of the C-terminal domains. Several conformational changes between the ATP- and ADP-bound states explain the coupling of ATP hydrolysis to RNA translocation, mainly mediated by a beta-turn of the RecA1 domain containing the identified RF motif. This mechanism is clearly different to those of other RNA helicases. Prp43 adopts an open conformation after ATP binding and switches into the closed conformation after binding to RNA. Active site structures, localization of the Hook-Turn in the RecA1 domain and of the Hook-Loop in the RecA2 domain in the ctPrp43DELTAN-U7-ADP-BeF3- complex structure
additional information
structure-function analysis of Frh, three-dimensional structure modelling, detailed overview. Structure comparisons to the yeast homologue Mtr4 reveal structure differences and the distinct role of FRH in the clock. The KOW module at an exposed position within a positively charged patch of residues that include K811, K731, R812, K766, R806, K739, R831, R832, and K824. Key residues for FRH function are: K208 and S324 compose the ATP-binding site, E294 lies between the ADP and RNA pockets and participates in ATP hydrolysis, P871 resides in the elbow region of the arch domain. K811, R806, R712, and K766 contribute to a positively charged surface on the KOW domain module. R806H disrupts the clock. Q131, G132, and V142 in the N-terminus provide interactions to the helicase RecA domains. Analysis of interactions analysis of the N-terminal FRQ interaction region, and of interactions of the KOW module with clock components
additional information
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structure-function analysis of Frh, three-dimensional structure modelling, detailed overview. Structure comparisons to the yeast homologue Mtr4 reveal structure differences and the distinct role of FRH in the clock. The KOW module at an exposed position within a positively charged patch of residues that include K811, K731, R812, K766, R806, K739, R831, R832, and K824. Key residues for FRH function are: K208 and S324 compose the ATP-binding site, E294 lies between the ADP and RNA pockets and participates in ATP hydrolysis, P871 resides in the elbow region of the arch domain. K811, R806, R712, and K766 contribute to a positively charged surface on the KOW domain module. R806H disrupts the clock. Q131, G132, and V142 in the N-terminus provide interactions to the helicase RecA domains. Analysis of interactions analysis of the N-terminal FRQ interaction region, and of interactions of the KOW module with clock components
additional information
the C-terminal domain of Ded1 (amino acids 536-604) is a low complexity sequence that is necessary for the interaction with eIF4G1 and for self-association and the formation of Ded1 oligomers
additional information
the C-terminal region of the RNA helicase CshA is required for the interaction with the degradosome and turnover of bulk RNA in the opportunistic pathogen Staphylococcus aureus. Half-lives of diverse RNAs in the wild-type and mutant CshA strains, correlation of half life and steady-state levels, detailed overview
additional information
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the C-terminal region of the RNA helicase CshA is required for the interaction with the degradosome and turnover of bulk RNA in the opportunistic pathogen Staphylococcus aureus. Half-lives of diverse RNAs in the wild-type and mutant CshA strains, correlation of half life and steady-state levels, detailed overview
additional information
the DEAD motif is critical for T3SS gene expression. DeaD-dependent activation of ExsA translation is specific to the exsA coding sequence and native Shine-Dalgarno sequence
additional information
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the DEAD motif is critical for T3SS gene expression. DeaD-dependent activation of ExsA translation is specific to the exsA coding sequence and native Shine-Dalgarno sequence
additional information
the long, flexible C-terminal regions of CsdA are essential for high enzymatic activity and strong RNA-binding affinity, and the RNA-binding domain prefers binding single-stranded G-rich RNA. CsdA functions as a stable dimer at low temperature. The C-terminal regions are critical for RNA binding and efficient enzymatic activities. CsdA_RBD can specifically bind to the regions with a preference for single-stranded G-rich RNA, which may help to bring the helicase core to unwind the adjacent duplex, structure of dimeric RNA helicase CsdA and indispensable role of its C-terminal regions, overview
additional information
the N-terminal RecA-like domain 1 (amino acids 1-211) of DEAD-box RNA helicase CshA adopts a conserved alpha/beta RecA-like structure with seven parallel strands surrounded by nine alpha-helices. The Q motif and motif I are responsible for the binding of the adenine group and phosphate group of AMP, respectively. Motif I undergoes a conformational change upon AMP binding. Essential roles of Phe22 in the Q motif and Lys52 in motif I for binding ATP, indicating a conserved substrate-binding mechanism in SaCshA compared with other DEAD-box RNA helicases. Structure comparisons, overview
additional information
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the N-terminal RecA-like domain 1 (amino acids 1-211) of DEAD-box RNA helicase CshA adopts a conserved alpha/beta RecA-like structure with seven parallel strands surrounded by nine alpha-helices. The Q motif and motif I are responsible for the binding of the adenine group and phosphate group of AMP, respectively. Motif I undergoes a conformational change upon AMP binding. Essential roles of Phe22 in the Q motif and Lys52 in motif I for binding ATP, indicating a conserved substrate-binding mechanism in SaCshA compared with other DEAD-box RNA helicases. Structure comparisons, overview
additional information
the RecA catalytic core houses DbpA's ATPase and helicase activities. DbpA contains an RNA binding domain, responsible for tight binding of DbpA to hairpin 92 of 23S ribosomal RNA, and a RecA-like catalytic core responsible for double-helix unwinding
additional information
the SF1 core of Aquarius consists of two RecA-like domains, an alpha-helical stalk and a beta-barrel domain. The canonical sequence motifs of RNA helicases are conserved, and the ATP analogue binds with the adenine sandwiched between Leu1157 and Ile800. The amino group of the adenine is recognized by Gln806 from the Q motif, a distinctive feature of helicases able to use only ATP. The space between the RecA1, RecA2, beta-barrel and a domain that we denote as an armadillo (ARM) domain is filled by the so-called stalk, a structural unit encompassing 125 residues (416-492 and 660-710) exhibiting helixadces, extensive coils and loops. The large surfaces that the stalk shares with other domains suggest that it has a key architectural role. Notably, numerous large hydrophobic residues that mediate these contacts are highly conxadserved. Aquarius's ARM domain is required for intron-binding complex (IBC) formation
additional information
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the SF1 core of Aquarius consists of two RecA-like domains, an alpha-helical stalk and a beta-barrel domain. The canonical sequence motifs of RNA helicases are conserved, and the ATP analogue binds with the adenine sandwiched between Leu1157 and Ile800. The amino group of the adenine is recognized by Gln806 from the Q motif, a distinctive feature of helicases able to use only ATP. The space between the RecA1, RecA2, beta-barrel and a domain that we denote as an armadillo (ARM) domain is filled by the so-called stalk, a structural unit encompassing 125 residues (416-492 and 660-710) exhibiting helixadces, extensive coils and loops. The large surfaces that the stalk shares with other domains suggest that it has a key architectural role. Notably, numerous large hydrophobic residues that mediate these contacts are highly conxadserved. Aquarius's ARM domain is required for intron-binding complex (IBC) formation
additional information
the structure of Brr2 differs decisively from that of other spliceosomal helicases, enzyme structure analysis, detailed overview. Comparison of human and yeast enzymes, comparative modeling
additional information
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the structure of Brr2 differs decisively from that of other spliceosomal helicases, enzyme structure analysis, detailed overview. Comparison of human and yeast enzymes, comparative modeling
additional information
the structure of Brr2 differs decisively from that of other spliceosomal helicases, enzyme structure analysis, detailed overview. Comparison of human and yeast enzymes, comparative modeling. Analysis of the mechanism of spliceosome activation using multi-wavelength single-molecule co-localization spectroscopy demonstrates that after tri-snRNP binding, the spliceosome can either proceed to activation or release U4 and U5 snRNAs. The ATP-dependent loss of U4 and U5 snRNAs is suggested to represent Prp28-mediated displacement of the tri-snRNP
additional information
-
the structure of Brr2 differs decisively from that of other spliceosomal helicases, enzyme structure analysis, detailed overview. Comparison of human and yeast enzymes, comparative modeling. Analysis of the mechanism of spliceosome activation using multi-wavelength single-molecule co-localization spectroscopy demonstrates that after tri-snRNP binding, the spliceosome can either proceed to activation or release U4 and U5 snRNAs. The ATP-dependent loss of U4 and U5 snRNAs is suggested to represent Prp28-mediated displacement of the tri-snRNP
additional information
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the DEAD motif is critical for T3SS gene expression. DeaD-dependent activation of ExsA translation is specific to the exsA coding sequence and native Shine-Dalgarno sequence
-
additional information
Thermochaetoides thermophila IMI 039719
-
RNA loading mechanism of Prp43, overview. Prp43 binds RNA in a sequence-independent fashion. Analysis of crystal structures of Prp43 complexes in different functional states and the analysis of structure-based mutants providing insights into the unwinding and loading mechanism of RNAs. The Prp43-ATP-analogue-RNA complex shows the localization of the RNA inside a tunnel formed by the two RecA-like and C-terminal domains. In the ATP-bound state this tunnel can be transformed into a groove prone for RNA binding by large rearrangements of the C-terminal domains. Several conformational changes between the ATP- and ADP-bound states explain the coupling of ATP hydrolysis to RNA translocation, mainly mediated by a beta-turn of the RecA1 domain containing the identified RF motif. This mechanism is clearly different to those of other RNA helicases. Prp43 adopts an open conformation after ATP binding and switches into the closed conformation after binding to RNA. Active site structures, localization of the Hook-Turn in the RecA1 domain and of the Hook-Loop in the RecA2 domain in the ctPrp43DELTAN-U7-ADP-BeF3- complex structure
-
additional information
-
the C-terminal region of the RNA helicase CshA is required for the interaction with the degradosome and turnover of bulk RNA in the opportunistic pathogen Staphylococcus aureus. Half-lives of diverse RNAs in the wild-type and mutant CshA strains, correlation of half life and steady-state levels, detailed overview
-
additional information
-
mutational analysis shows that only the C-terminus of the RNA helicase CshA, representing the highly variable region of the molecule, is necessary for binding to sarA mRNA
-
additional information
Thermochaetoides thermophila DSM 1495
-
RNA loading mechanism of Prp43, overview. Prp43 binds RNA in a sequence-independent fashion. Analysis of crystal structures of Prp43 complexes in different functional states and the analysis of structure-based mutants providing insights into the unwinding and loading mechanism of RNAs. The Prp43-ATP-analogue-RNA complex shows the localization of the RNA inside a tunnel formed by the two RecA-like and C-terminal domains. In the ATP-bound state this tunnel can be transformed into a groove prone for RNA binding by large rearrangements of the C-terminal domains. Several conformational changes between the ATP- and ADP-bound states explain the coupling of ATP hydrolysis to RNA translocation, mainly mediated by a beta-turn of the RecA1 domain containing the identified RF motif. This mechanism is clearly different to those of other RNA helicases. Prp43 adopts an open conformation after ATP binding and switches into the closed conformation after binding to RNA. Active site structures, localization of the Hook-Turn in the RecA1 domain and of the Hook-Loop in the RecA2 domain in the ctPrp43DELTAN-U7-ADP-BeF3- complex structure
-
additional information
-
the DEAD motif is critical for T3SS gene expression. DeaD-dependent activation of ExsA translation is specific to the exsA coding sequence and native Shine-Dalgarno sequence
-
additional information
-
the DEAD motif is critical for T3SS gene expression. DeaD-dependent activation of ExsA translation is specific to the exsA coding sequence and native Shine-Dalgarno sequence
-
additional information
-
structure-function analysis of Frh, three-dimensional structure modelling, detailed overview. Structure comparisons to the yeast homologue Mtr4 reveal structure differences and the distinct role of FRH in the clock. The KOW module at an exposed position within a positively charged patch of residues that include K811, K731, R812, K766, R806, K739, R831, R832, and K824. Key residues for FRH function are: K208 and S324 compose the ATP-binding site, E294 lies between the ADP and RNA pockets and participates in ATP hydrolysis, P871 resides in the elbow region of the arch domain. K811, R806, R712, and K766 contribute to a positively charged surface on the KOW domain module. R806H disrupts the clock. Q131, G132, and V142 in the N-terminus provide interactions to the helicase RecA domains. Analysis of interactions analysis of the N-terminal FRQ interaction region, and of interactions of the KOW module with clock components
-
additional information
-
the N-terminal RecA-like domain 1 (amino acids 1-211) of DEAD-box RNA helicase CshA adopts a conserved alpha/beta RecA-like structure with seven parallel strands surrounded by nine alpha-helices. The Q motif and motif I are responsible for the binding of the adenine group and phosphate group of AMP, respectively. Motif I undergoes a conformational change upon AMP binding. Essential roles of Phe22 in the Q motif and Lys52 in motif I for binding ATP, indicating a conserved substrate-binding mechanism in SaCshA compared with other DEAD-box RNA helicases. Structure comparisons, overview
-
additional information
-
the DEAD motif is critical for T3SS gene expression. DeaD-dependent activation of ExsA translation is specific to the exsA coding sequence and native Shine-Dalgarno sequence
-
additional information
-
the DEAD motif is critical for T3SS gene expression. DeaD-dependent activation of ExsA translation is specific to the exsA coding sequence and native Shine-Dalgarno sequence
-
additional information
-
the DEAD motif is critical for T3SS gene expression. DeaD-dependent activation of ExsA translation is specific to the exsA coding sequence and native Shine-Dalgarno sequence
-
additional information
-
the C-terminal domain of Ded1 (amino acids 536-604) is a low complexity sequence that is necessary for the interaction with eIF4G1 and for self-association and the formation of Ded1 oligomers
-
additional information
-
the structure of Brr2 differs decisively from that of other spliceosomal helicases, enzyme structure analysis, detailed overview. Comparison of human and yeast enzymes, comparative modeling. Analysis of the mechanism of spliceosome activation using multi-wavelength single-molecule co-localization spectroscopy demonstrates that after tri-snRNP binding, the spliceosome can either proceed to activation or release U4 and U5 snRNAs. The ATP-dependent loss of U4 and U5 snRNAs is suggested to represent Prp28-mediated displacement of the tri-snRNP
-
additional information
-
structure-function analysis of Frh, three-dimensional structure modelling, detailed overview. Structure comparisons to the yeast homologue Mtr4 reveal structure differences and the distinct role of FRH in the clock. The KOW module at an exposed position within a positively charged patch of residues that include K811, K731, R812, K766, R806, K739, R831, R832, and K824. Key residues for FRH function are: K208 and S324 compose the ATP-binding site, E294 lies between the ADP and RNA pockets and participates in ATP hydrolysis, P871 resides in the elbow region of the arch domain. K811, R806, R712, and K766 contribute to a positively charged surface on the KOW domain module. R806H disrupts the clock. Q131, G132, and V142 in the N-terminus provide interactions to the helicase RecA domains. Analysis of interactions analysis of the N-terminal FRQ interaction region, and of interactions of the KOW module with clock components
-
additional information
-
structure-function analysis of Frh, three-dimensional structure modelling, detailed overview. Structure comparisons to the yeast homologue Mtr4 reveal structure differences and the distinct role of FRH in the clock. The KOW module at an exposed position within a positively charged patch of residues that include K811, K731, R812, K766, R806, K739, R831, R832, and K824. Key residues for FRH function are: K208 and S324 compose the ATP-binding site, E294 lies between the ADP and RNA pockets and participates in ATP hydrolysis, P871 resides in the elbow region of the arch domain. K811, R806, R712, and K766 contribute to a positively charged surface on the KOW domain module. R806H disrupts the clock. Q131, G132, and V142 in the N-terminus provide interactions to the helicase RecA domains. Analysis of interactions analysis of the N-terminal FRQ interaction region, and of interactions of the KOW module with clock components
-
additional information
-
structure-function analysis of Frh, three-dimensional structure modelling, detailed overview. Structure comparisons to the yeast homologue Mtr4 reveal structure differences and the distinct role of FRH in the clock. The KOW module at an exposed position within a positively charged patch of residues that include K811, K731, R812, K766, R806, K739, R831, R832, and K824. Key residues for FRH function are: K208 and S324 compose the ATP-binding site, E294 lies between the ADP and RNA pockets and participates in ATP hydrolysis, P871 resides in the elbow region of the arch domain. K811, R806, R712, and K766 contribute to a positively charged surface on the KOW domain module. R806H disrupts the clock. Q131, G132, and V142 in the N-terminus provide interactions to the helicase RecA domains. Analysis of interactions analysis of the N-terminal FRQ interaction region, and of interactions of the KOW module with clock components
-
additional information
Thermochaetoides thermophila CBS 144.50
-
RNA loading mechanism of Prp43, overview. Prp43 binds RNA in a sequence-independent fashion. Analysis of crystal structures of Prp43 complexes in different functional states and the analysis of structure-based mutants providing insights into the unwinding and loading mechanism of RNAs. The Prp43-ATP-analogue-RNA complex shows the localization of the RNA inside a tunnel formed by the two RecA-like and C-terminal domains. In the ATP-bound state this tunnel can be transformed into a groove prone for RNA binding by large rearrangements of the C-terminal domains. Several conformational changes between the ATP- and ADP-bound states explain the coupling of ATP hydrolysis to RNA translocation, mainly mediated by a beta-turn of the RecA1 domain containing the identified RF motif. This mechanism is clearly different to those of other RNA helicases. Prp43 adopts an open conformation after ATP binding and switches into the closed conformation after binding to RNA. Active site structures, localization of the Hook-Turn in the RecA1 domain and of the Hook-Loop in the RecA2 domain in the ctPrp43DELTAN-U7-ADP-BeF3- complex structure
-
additional information
-
the N-terminal RecA-like domain 1 (amino acids 1-211) of DEAD-box RNA helicase CshA adopts a conserved alpha/beta RecA-like structure with seven parallel strands surrounded by nine alpha-helices. The Q motif and motif I are responsible for the binding of the adenine group and phosphate group of AMP, respectively. Motif I undergoes a conformational change upon AMP binding. Essential roles of Phe22 in the Q motif and Lys52 in motif I for binding ATP, indicating a conserved substrate-binding mechanism in SaCshA compared with other DEAD-box RNA helicases. Structure comparisons, overview
-
additional information
-
the DEAD motif is critical for T3SS gene expression. DeaD-dependent activation of ExsA translation is specific to the exsA coding sequence and native Shine-Dalgarno sequence
-
additional information
-
structure-function analysis of Frh, three-dimensional structure modelling, detailed overview. Structure comparisons to the yeast homologue Mtr4 reveal structure differences and the distinct role of FRH in the clock. The KOW module at an exposed position within a positively charged patch of residues that include K811, K731, R812, K766, R806, K739, R831, R832, and K824. Key residues for FRH function are: K208 and S324 compose the ATP-binding site, E294 lies between the ADP and RNA pockets and participates in ATP hydrolysis, P871 resides in the elbow region of the arch domain. K811, R806, R712, and K766 contribute to a positively charged surface on the KOW domain module. R806H disrupts the clock. Q131, G132, and V142 in the N-terminus provide interactions to the helicase RecA domains. Analysis of interactions analysis of the N-terminal FRQ interaction region, and of interactions of the KOW module with clock components
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A115C/D262C
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site-directed mutagenesis, the mutant shows activity, structure and substrate specificity similar to the wild-type
A115C/E224C
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site-directed mutagenesis, the mutant shows activity, structure and substrate specificity similar to the wild-type
A115C/S229C
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site-directed mutagenesis, the mutant shows activity, structure and substrate specificity similar to the wild-type
S108C/E224C
-
site-directed mutagenesis, the mutant shows activity, structure and substrate specificity similar to the wild-type
S108C/S229C
-
site-directed mutagenesis, the mutant shows activity, structure and substrate specificity similar to the wild-type
D755A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 90% reduced ATPase activity compared to the wild-type enzyme
F788A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 30% reduced ATPase activity compared to the wild-type enzyme
G781S
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 75% reduced ATPase activity compared to the wild-type enzyme
H903A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 45% reduced ATPase activity compared to the wild-type enzyme
K691A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 80% reduced ATPase activity compared to the wild-type enzyme
Q785A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 65% reduced ATPase activity compared to the wild-type enzyme
Q785E
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 75% reduced ATPase activity compared to the wild-type enzyme
R791A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 10% increased ATPase activity compared to the wild-type enzyme
R815L
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 60% increased ATPase activity compared to the wild-type enzyme
R938A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 45% reduced ATPase activity compared to the wild-type enzyme
S790A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 60% reduced ATPase activity compared to the wild-type enzyme
S790W
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows 70% reduced ATPase activity compared to the wild-type enzyme
T812A/Y813A
-
site-directed mutagenesis, mutation in the conserved BMV 1a protein helicase motif, the mutant shows abolished RNA recruitment and RNA stabilization, and thus RNA replication function, but normal accumulation, localization, and 2apol recruitment, the mutant shows unaltered ATPase activity compared to the wild-type enzyme
H51A
-
site-directed mutagenesis, the mutant has an inactivated protease domain showing enhanced RNA helicase compared to wild-type full-length enzyme
R184Q/K185N/R186G/K187N
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construction of the N-terminally truncated mutant NS3DELTA180 containing a mutated RNA substrate biding motif, the mutant shows reduced RTPase activity
D310H
-
site-directed mutagenesis of the V motif, leads to altered enzyme activity, overview
D313H
-
site-directed mutagenesis of the V motif, leads to altered enzyme activity, overview
H320D
-
site-directed mutagenesis of the V motif, leads to altered enzyme activity, overview
Y383A
-
site-directed mutagenesis, the mutation causes the formation of a higher order molecular weight species in binding of RNaseE by RhlB
H293A
-
mutation results in a protein with a significantly higher level of ATPase in the absence of RNA. The mutant protein still unwinds RNA. In the presence of RNA, the H293A mutant hydrolyzes ATP slower than wild-type
D279A
site-directed mutagenesis, the mutation affects ATP hydrolysis
DELTA53-105
-
a region within the N-terminus of RHAU, referred to as the RSM, interacts with human telomerase RNA
F192E
site-directed mutagenesis, the mutant shows slightly reduced activity compared with the wild-type enzyme. Upf1F192E definitely prefers to unwind a dsDNA than to translocate it, strand switching
K191S
site-directed mutagenesis, the mutation affects ATP binding
K235A
site-directed mutagenesis of a conserved Lys residue in RNA binding domain dsRBD2, the mutation does not prevent purified full-length RNA helicase A from binding and unwinding duplex RNA in vitro, but efficiently inhibits RNA helicase A-stimulated HIV-1 RNA metabolism including the accumulation of viral mRNA and tRNALys3 annealing to viral RNA
K236A
site-directed mutagenesis of a conserved Lys residue in RNA binding domain dsRBD2, the mutation does not prevent purified full-length RNA helicase A from binding and unwinding duplex RNA in vitro, but efficiently inhibits RNA helicase A-stimulated HIV-1 RNA metabolism including the accumulation of viral mRNA and tRNALys3 annealing to viral RNA
K236E
-
mutant exhibits relatively minor reduction in interaction with SNV PCE
K50R
site-directed mutagenesis, ATPase dead mutant, fails completely to unwind triplex substrates
K54A
site-directed mutagenesis of a conserved Lys residue in RNA binding domain dsRBD1, the mutation does not prevent purified full-length RNA helicase A from binding and unwinding duplex RNA in vitro, but efficiently inhibits RNA helicase A-stimulated HIV-1 RNA metabolism including the accumulation of viral mRNA and tRNALys3 annealing to viral RNA
K54A/K55A
-
mutant exhibits relatively minor reduction in interaction with SNV PCE
K54A/K55A/K236E
-
triple mutant shows a severe reduction in interaction with junD post-transcriptional control element (PCE) or SNV PCE compared with wild-type
K55A
site-directed mutagenesis of a conserved Lys residue in RNA binding domain dsRBD1, the mutation does not prevent purified full-length RNA helicase A from binding and unwinding duplex RNA in vitro, but efficiently inhibits RNA helicase A-stimulated HIV-1 RNA metabolism including the accumulation of viral mRNA and tRNALys3 annealing to viral RNA
K829A
site-directed mutagenesis, mutation of the invariant lysine residue from motif I involved in ATP binding and hydrolysis drastically reduced Aquarius's ability to bind ATP and ADP and to hydroxadlyze ATP, the mutant shows significantly reduced ATPase activity compared to wild-type enzyme
K897del
site-directed mutagenesis, the mutant fails in unwinding the DNA substrates
Y1196A
site-directed mutagenesis, mutation of a conserved aromatic residue located near the putative RNA-binding surface of the RecA2 inhibits Aquarius's RNA-unwinding activity without changing its RNA-binding and ATPase properties, a helicase-deficient mutant
Y593F
-
expression of the mutant enzyme in SW620 cells leads to Snail repression, E-cadherin upregulation and vimentin repression
G199A
mutation in WALKER A motif, PCR-based mutagenesis, ATPase and RNA helicase activity lost
G460A
mutation of residues of the arginine finger within the active sites of ATP hydrolysis, no effect on either ATPase or RNA-unwinding activities
G463A
mutation of residues of the arginine finger within the active sites of ATP hydrolysis, no effect on either ATPase or RNA-unwinding activities
K200A
mutation in WALKER A motif, PCR-based mutagenesis, ATPase and RNA helicase activity lost
K200D
PCR-based mutagenesis, ATPase and RNA helicase activity lost
K200E
PCR-based mutagenesis, ATPase and RNA helicase activity lost
K200H
PCR-based mutagenesis, ATPase and RNA helicase activity lost
K200N
PCR-based mutagenesis, ATPase and RNA helicase activity lost
K200Q
PCR-based mutagenesis, ATPase and RNA helicase activity lost
K200R
PCR-based mutagenesis, ATPase and RNA helicase activity lost
Q457A
mutation of residues of the arginine finger within the active sites of ATP hydrolysis, 80% reduction of ATPase activity, no RNA helicase activity
R458A
mutation of residues of the arginine finger within the active sites of ATP hydrolysis, 90% reduction of ATPase activity, no RNA helicase activity
R459A
mutation of residues of the arginine finger within the active sites of ATP hydrolysis, no effect on either ATPase or RNA-unwinding activities
R461A
mutation of residues of the arginine finger within the active sites of ATP hydrolysis, no ATPase activity, no RNA helicase activity
R464A
mutation of residues of the arginine finger within the active sites of ATP hydrolysis, no ATPase activity, no RNA helicase activity
T201A
mutation in WALKER A motif, PCR-based mutagenesis, ATPase and RNA helicase activity lost
V462A
mutation of residues of the arginine finger within the active sites of ATP hydrolysis, no effect on either ATPase or RNA-unwinding activities
R806H
site-directed mutagenesis, the mutation resides in a positively charged surface of the KOW domain, far removed from the helicase core, and disrupts circadian rhythms
V142G
site-directed mutagenesis, the substitution near the N-terminus alters protein complex of frequency (FRQ) and white-collar complex (WCC)binding to FRH, but produces an unusual short clock period
R806H
-
site-directed mutagenesis, the mutation resides in a positively charged surface of the KOW domain, far removed from the helicase core, and disrupts circadian rhythms
-
V142G
-
site-directed mutagenesis, the substitution near the N-terminus alters protein complex of frequency (FRQ) and white-collar complex (WCC)binding to FRH, but produces an unusual short clock period
-
R806H
-
site-directed mutagenesis, the mutation resides in a positively charged surface of the KOW domain, far removed from the helicase core, and disrupts circadian rhythms
-
V142G
-
site-directed mutagenesis, the substitution near the N-terminus alters protein complex of frequency (FRQ) and white-collar complex (WCC)binding to FRH, but produces an unusual short clock period
-
R806H
-
site-directed mutagenesis, the mutation resides in a positively charged surface of the KOW domain, far removed from the helicase core, and disrupts circadian rhythms
-
V142G
-
site-directed mutagenesis, the substitution near the N-terminus alters protein complex of frequency (FRQ) and white-collar complex (WCC)binding to FRH, but produces an unusual short clock period
-
R806H
-
site-directed mutagenesis, the mutation resides in a positively charged surface of the KOW domain, far removed from the helicase core, and disrupts circadian rhythms
-
V142G
-
site-directed mutagenesis, the substitution near the N-terminus alters protein complex of frequency (FRQ) and white-collar complex (WCC)binding to FRH, but produces an unusual short clock period
-
R806H
-
site-directed mutagenesis, the mutation resides in a positively charged surface of the KOW domain, far removed from the helicase core, and disrupts circadian rhythms
-
V142G
-
site-directed mutagenesis, the substitution near the N-terminus alters protein complex of frequency (FRQ) and white-collar complex (WCC)binding to FRH, but produces an unusual short clock period
-
R806H
-
interacts with the circadian oscillator component FREQUENCY (FRQ), but interaction between the FRQFRHR806H complex (FFC) and White Collar Complex is severely affected
E168A
site-directed mutagenesis, the mutation eliminates ATP hydrolysis and helicase activity, and the mutant is unable to restore PexsD-lacZ activity to levels observed with wild-type DeaD
E168Q
site-directed mutagenesis, the mutation eliminates ATP hydrolysis and helicase activity, and the mutant is unable to restore PexsD-lacZ activity to levels observed with wild-type DeaD
E168A
-
site-directed mutagenesis, the mutation eliminates ATP hydrolysis and helicase activity, and the mutant is unable to restore PexsD-lacZ activity to levels observed with wild-type DeaD
-
E168Q
-
site-directed mutagenesis, the mutation eliminates ATP hydrolysis and helicase activity, and the mutant is unable to restore PexsD-lacZ activity to levels observed with wild-type DeaD
-
E168A
-
site-directed mutagenesis, the mutation eliminates ATP hydrolysis and helicase activity, and the mutant is unable to restore PexsD-lacZ activity to levels observed with wild-type DeaD
-
E168Q
-
site-directed mutagenesis, the mutation eliminates ATP hydrolysis and helicase activity, and the mutant is unable to restore PexsD-lacZ activity to levels observed with wild-type DeaD
-
E168A
-
site-directed mutagenesis, the mutation eliminates ATP hydrolysis and helicase activity, and the mutant is unable to restore PexsD-lacZ activity to levels observed with wild-type DeaD
-
E168Q
-
site-directed mutagenesis, the mutation eliminates ATP hydrolysis and helicase activity, and the mutant is unable to restore PexsD-lacZ activity to levels observed with wild-type DeaD
-
E168A
-
site-directed mutagenesis, the mutation eliminates ATP hydrolysis and helicase activity, and the mutant is unable to restore PexsD-lacZ activity to levels observed with wild-type DeaD
-
E168Q
-
site-directed mutagenesis, the mutation eliminates ATP hydrolysis and helicase activity, and the mutant is unable to restore PexsD-lacZ activity to levels observed with wild-type DeaD
-
E168A
-
site-directed mutagenesis, the mutation eliminates ATP hydrolysis and helicase activity, and the mutant is unable to restore PexsD-lacZ activity to levels observed with wild-type DeaD
-
E168Q
-
site-directed mutagenesis, the mutation eliminates ATP hydrolysis and helicase activity, and the mutant is unable to restore PexsD-lacZ activity to levels observed with wild-type DeaD
-
E168A
-
site-directed mutagenesis, the mutation eliminates ATP hydrolysis and helicase activity, and the mutant is unable to restore PexsD-lacZ activity to levels observed with wild-type DeaD
-
E168Q
-
site-directed mutagenesis, the mutation eliminates ATP hydrolysis and helicase activity, and the mutant is unable to restore PexsD-lacZ activity to levels observed with wild-type DeaD
-
E168A
-
site-directed mutagenesis, the mutation eliminates ATP hydrolysis and helicase activity, and the mutant is unable to restore PexsD-lacZ activity to levels observed with wild-type DeaD
-
E168Q
-
site-directed mutagenesis, the mutation eliminates ATP hydrolysis and helicase activity, and the mutant is unable to restore PexsD-lacZ activity to levels observed with wild-type DeaD
-
E909K
site-directed mutagenesis, the temperature-sensitive mutant, encoded by the slt22-1 allele, is synthetically lethal with mutations in U2 or U6 snRNAs that affect the stability or conformation of U2/U6 helix II. The ATPase activity of this variant is no longer stimulated by a U2/ U6 duplex, it is proposed that Brr2 might proofread U2/U6 interactions. The E909K exchange in Brr2 blocks splicing in extracts at or before the first catalytic step and leads to the appearance of an off-pathway spliceosomal particle following B complex formation, which lacks U4 and U5 snRNAs
F162A
kcat/KM for ATP is 1% of wild-type value
F162L
kcat/KM for ATP is 25% of wild-type value
G858R
site-directed mutagenesis, the mutant shows differing cross-linking profiles compared to wild-type Brr2, the mutation is in the NC 5'HP/separator loop with U6 snRNA
K177A
mutant enzyme shows no stimulation of ATPase activity by single-stranded RNA
Q169A
kcat/KM for ATP is 0.3% of wild-type value
Q169E
kcat/KM for ATP is 0.4% of wild-type value
R681C
site-directed mutagenesis, a brr2 mutation linked to the RP33 form of autosomal dominant retinitis pigmentosa, it maps to the linker between the RecA domains of the NC, the mutation leads to altered Brr2 ATPase activity and aberrant partitioning of spliceosomes along activation and discard pathways
R681H
site-directed mutagenesis, a brr2 mutation linked to the RP33 form of autosomal dominant retinitis pigmentosa, it maps to the linker between the RecA domains of the NC, the mutation leads to altered Brr2 ATPase activity and aberrant partitioning of spliceosomes along activation and discard pathways
T166A
kcat/KM for ATP is 37% of wild-type value
T166S
kcat/KM for ATP is 26% of wild-type value
V683L
site-directed mutagenesis, a brr2 mutation linked to the RP33 form of autosomal dominant retinitis pigmentosa, it maps to the linker between the RecA domains of the NC, the mutation leads to altered Brr2 ATPase activity and aberrant partitioning of spliceosomes along activation and discard pathways
Y689C
site-directed mutagenesis, a brr2 mutation linked to the RP33 form of autosomal dominant retinitis pigmentosa, it maps to the beginning of the RecA2 domain
E909K
-
site-directed mutagenesis, the temperature-sensitive mutant, encoded by the slt22-1 allele, is synthetically lethal with mutations in U2 or U6 snRNAs that affect the stability or conformation of U2/U6 helix II. The ATPase activity of this variant is no longer stimulated by a U2/ U6 duplex, it is proposed that Brr2 might proofread U2/U6 interactions. The E909K exchange in Brr2 blocks splicing in extracts at or before the first catalytic step and leads to the appearance of an off-pathway spliceosomal particle following B complex formation, which lacks U4 and U5 snRNAs
-
G858R
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site-directed mutagenesis, the mutant shows differing cross-linking profiles compared to wild-type Brr2, the mutation is in the NC 5'HP/separator loop with U6 snRNA
-
R681C
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site-directed mutagenesis, a brr2 mutation linked to the RP33 form of autosomal dominant retinitis pigmentosa, it maps to the linker between the RecA domains of the NC, the mutation leads to altered Brr2 ATPase activity and aberrant partitioning of spliceosomes along activation and discard pathways
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R681H
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site-directed mutagenesis, a brr2 mutation linked to the RP33 form of autosomal dominant retinitis pigmentosa, it maps to the linker between the RecA domains of the NC, the mutation leads to altered Brr2 ATPase activity and aberrant partitioning of spliceosomes along activation and discard pathways
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V683L
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site-directed mutagenesis, a brr2 mutation linked to the RP33 form of autosomal dominant retinitis pigmentosa, it maps to the linker between the RecA domains of the NC, the mutation leads to altered Brr2 ATPase activity and aberrant partitioning of spliceosomes along activation and discard pathways
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E300A
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mutation causes severe defect in RNA unwinding that correlates with reduced rate of ATP hydrolysis
H299A
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mutation elicits defects in RNA unwinding but spares the ATPase activity
K191A
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mutation causes severe defect in RNA unwinding that correlates with reduced rate of ATP hydrolysis
R229A
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mutation causes severe defect in RNA unwinding that correlates with reduced rate of ATP hydrolysis
T192A
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mutation causes severe defect in RNA unwinding that correlates with reduced rate of ATP hydrolysis
T326A
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mutation elicits defects in RNA unwinding but spares the ATPase activity
T328A
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mutation elicits defects in RNA unwinding but spares the ATPase activity
D172A
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the ration of (kcat/Km)ATP/(kcat/Km)GTP is 41% of the ratio determined for the wild-type enzyme
E169A
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the ration of (kcat/Km)ATP/(kcat/Km)GTP is 38% of the ratio determined for the wild-type enzyme
E173A
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the ration of (kcat/Km)ATP/(kcat/Km)GTP is 17% of the ratio determined for the wild-type enzyme
E180A
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the ration of (kcat/Km)ATP/(kcat/Km)GTP is 35% of the ratio determined for the wild-type enzyme
E182A
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the ration of (kcat/Km)ATP/(kcat/Km)GTP is 29% of the ratio determined for the wild-type enzyme
F179A
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the ration of (kcat/Km)ATP/(kcat/Km)GTP is 19% of the ratio determined for the wild-type enzyme
K186A
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the ration of (kcat/Km)ATP/(kcat/Km)GTP is 15% of the ratio determined for the wild-type enzyme
K187A
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the ration of (kcat/Km)ATP/(kcat/Km)GTP is 8% of the ratio determined for the wild-type enzyme
Q188A
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the ration of (kcat/Km)ATP/(kcat/Km)GTP is 33% of the ratio determined for the wild-type enzyme
R170A
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the ration of (kcat/Km)ATP/(kcat/Km)GTP is 31% of the ratio determined for the wild-type enzyme
R185A
-
inactive mutant enzyme
K232A
site-directed mutagenesis in the helicase domain of NS3
K232A
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site-directed mutagenesis in the helicase domain of NS3
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K199A/T200A
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site-directed mutagenesis, mutant avoid of basal and of RNA-stimulated NTPase activity
K199A/T200A
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site-directed mutagenesis, the mutation in the C-terminal domain of NS3 eliminates both the basal and the RNA-stimulated NTPase activity
K199A/T200A
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site-directed mutagenesis, mutant avoid of basal and of RNA-stimulated NTPase activity
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K199A/T200A
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site-directed mutagenesis, the mutation in the C-terminal domain of NS3 eliminates both the basal and the RNA-stimulated NTPase activity
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M1708A
NS3-4A construct, ability to bind and unwind RNA in vitro, mutation reduces functional NS3-4A binding affinity for RNA by 500-fold relative to the wild-type
M1708A
site-directed mutagenesis, the NS3-4A mutant shows decreased ATPase activity and reduced RNA stimulation activity compared to wild-type NS3
S1369R
NS3-4A construct, suppressor mutant, ATP-coupled RNA affinity identical to that of wild-type NS3-4A
S1369R
site-directed mutagenesis, the NS3-4A mutant shows increased ATPase activity and RNA stimulation activity compared to wild-type NS3
S1369R/M1708A
NS3-4A construct, reduced ATP-coupled RNA affinity of the single mutant suppressed by the addition of the S1369R mutation
S1369R/M1708A
site-directed mutagenesis, the NS3-4A mutant shows increased ATPase activity and reduced RNA stimulation activity compared to wild-type NS3
S1369R/Y1702A
NS3-4A construct, reduced ATP-coupled RNA affinity of the single mutant suppressed by the addition of the S1369R mutation
S1369R/Y1702A
site-directed mutagenesis, the NS3-4A mutant shows decreased ATPase activity and reduced RNA stimulation activity compared to wild-type NS3
Y1702A
NS3-4A construct, ability to bind and unwind RNA in vitro, mutation reduces functional NS3-4A binding affinity for RNA by 500-fold relative to the wild-type
Y1702A
site-directed mutagenesis, the NS3-4A mutant shows decreased ATPase activity and reduced RNA stimulation activity compared to wild-type NS3
additional information
construction of double knockdown mutant rh3-4/clpr2-1, chloroplast rps12-int1 splicing defects in mutant rh3-4
additional information
generation of RH7 knockout mutant lines, several morphological alterations such as disturbed vein pattern, pointed first true leaves, and short roots, which resemble ribosome-related mutants of Arabidopsis thaliana, phenotype analysis of rh7-5 and rh7-8 mutants under 22°C, overview. Knockout mutants of AtRH7 display several morphological alterations during vegetative and reproductive growth. In addition, the mutants exhibit severe defects in germination and leaf development under long-term low temperature conditions. Accumulation of rRNA precursors in rh7 mutant plants corroborate the hypothesis that AtRH7 affects ribosome biogenesis. AtRH7 mutations affect ribosomal RNA biogenesis in the nucleolus
additional information
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generation of RH7 knockout mutant lines, several morphological alterations such as disturbed vein pattern, pointed first true leaves, and short roots, which resemble ribosome-related mutants of Arabidopsis thaliana, phenotype analysis of rh7-5 and rh7-8 mutants under 22°C, overview. Knockout mutants of AtRH7 display several morphological alterations during vegetative and reproductive growth. In addition, the mutants exhibit severe defects in germination and leaf development under long-term low temperature conditions. Accumulation of rRNA precursors in rh7 mutant plants corroborate the hypothesis that AtRH7 affects ribosome biogenesis. AtRH7 mutations affect ribosomal RNA biogenesis in the nucleolus
additional information
virus-induced ISE2 gene silencing, TRV constructs are introduced into Agrobacterium strain GV3101 for plant infiltrations. Loss of ISE2 compromises C-to-U RNA editing at specific sites. Total RNA is isolated from leaves of the same age as the ISE2-SUP leaves analyzed, and RNA editing at the six candidate ISE2-specific sites and several unaffected sites is measured. The clpP1-559 site exhibited reduced RNA editing efficiency in both the ISE2-SUP and the var2-2 leaves, but the extent of RNA editing in ISE2-SUP leaves (25%) is less than half of that in var2-2 leaves (59%). Thus, depletion of ISE2 has a more drastic effect on the RNA editing efficiency at the clpP1-559 site than depletion of FTSH2. Similarly, while the var2-2 mutant displays decreased RNA editing at petL-5 and rpoA-200, the decrease at those sites is more drastic in ISE2-SUP leaves than in var2-2 leaves. Accumulation of chloroplast mRNAs is altered in the absence of ISE2
additional information
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virus-induced ISE2 gene silencing, TRV constructs are introduced into Agrobacterium strain GV3101 for plant infiltrations. Loss of ISE2 compromises C-to-U RNA editing at specific sites. Total RNA is isolated from leaves of the same age as the ISE2-SUP leaves analyzed, and RNA editing at the six candidate ISE2-specific sites and several unaffected sites is measured. The clpP1-559 site exhibited reduced RNA editing efficiency in both the ISE2-SUP and the var2-2 leaves, but the extent of RNA editing in ISE2-SUP leaves (25%) is less than half of that in var2-2 leaves (59%). Thus, depletion of ISE2 has a more drastic effect on the RNA editing efficiency at the clpP1-559 site than depletion of FTSH2. Similarly, while the var2-2 mutant displays decreased RNA editing at petL-5 and rpoA-200, the decrease at those sites is more drastic in ISE2-SUP leaves than in var2-2 leaves. Accumulation of chloroplast mRNAs is altered in the absence of ISE2
additional information
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virus-induced ISE2 gene silencing, TRV constructs are introduced into Agrobacterium strain GV3101 for plant infiltrations. Loss of ISE2 compromises C-to-U RNA editing at specific sites. Total RNA is isolated from leaves of the same age as the ISE2-SUP leaves analyzed, and RNA editing at the six candidate ISE2-specific sites and several unaffected sites is measured. The clpP1-559 site exhibited reduced RNA editing efficiency in both the ISE2-SUP and the var2-2 leaves, but the extent of RNA editing in ISE2-SUP leaves (25%) is less than half of that in var2-2 leaves (59%). Thus, depletion of ISE2 has a more drastic effect on the RNA editing efficiency at the clpP1-559 site than depletion of FTSH2. Similarly, while the var2-2 mutant displays decreased RNA editing at petL-5 and rpoA-200, the decrease at those sites is more drastic in ISE2-SUP leaves than in var2-2 leaves. Accumulation of chloroplast mRNAs is altered in the absence of ISE2
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additional information
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trans interference by BMV 1a protein helicase mutants with BMV 1a protein-stimulated RNA3 accumulation, overview
additional information
knockdown of hel-1 specifically decreases daf-2(-)-mediated longevity in an RNAi-hypersensitive rrf-3(pk1426) mutant background. hel-1 RNAi has a robust and specific effect on the longevity of daf-2 mutants. Resistance to heat stress is not affected by hel-1 mutations or RNAi, effects of hel-1 RNAi and hel-1 mutations on resistance to pathogenic bacteria (Pseudomonas aeruginosa, PA14) and oxidative stress are variable
additional information
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knockdown of hel-1 specifically decreases daf-2(-)-mediated longevity in an RNAi-hypersensitive rrf-3(pk1426) mutant background. hel-1 RNAi has a robust and specific effect on the longevity of daf-2 mutants. Resistance to heat stress is not affected by hel-1 mutations or RNAi, effects of hel-1 RNAi and hel-1 mutations on resistance to pathogenic bacteria (Pseudomonas aeruginosa, PA14) and oxidative stress are variable
additional information
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for the truncated NS3 helicase domain both NTPase and helicase activities are up-regulated by NS5B, for the full-length NS3, the NTPase activity, but not the helicase activity, is stimulated by NS5B, specific interaction between NS3 and NS5B
additional information
for the truncated NS3 helicase domain both NTPase and helicase activities are up-regulated by NS5B, for the full-length NS3, the NTPase activity, but not the helicase activity, is stimulated by NS5B, specific interaction between NS3 and NS5B
additional information
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for the truncated NS3 helicase domain both NTPase and helicase activities are up-regulated by NS5B, for the full-length NS3, the NTPase activity, but not the helicase activity, is stimulated by NS5B, specific interaction between NS3 and NS5B
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additional information
ddx27 mutant zebrafish show skeletal muscle abnormalities. Overexpression of human DDX27 mRNA results in a significant decrease in mutant zebrafish phenotype
additional information
depletion of the enzyme gene expression by RNAi in both glia and clock neurons, knockdown of belle with the pan-glial driver repo-Gal4 and lama-Gal4, a driver for glial precursor cells, lamina precursor cells and lamina neurons. The belEY08943 mutant exhibits a less striking phenotype: a significant difference was observed in the PDF positive s-LNvs only in constant darkness, where the oscillation of PER is 4 h delayed compared to control, similarly to what described in belcap-1 flies. Both belle mutants are characterized by a reduction in the number of l-LNvs: a high percentage of brains, in fact, presented three neurons instead of the canonical four (83.93, 76.28, and 6.78% in bel cap-1, bel EY08943, and white 1118, respectively). In contrast, RNAi against belle in the photoreceptor cells (GMR-Gal4 and ninaE-Gal4) does not affect either vitality or behavior. Locomotor activity of belle knockdown flies under different conditions, overview
additional information
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depletion of the enzyme gene expression by RNAi in both glia and clock neurons, knockdown of belle with the pan-glial driver repo-Gal4 and lama-Gal4, a driver for glial precursor cells, lamina precursor cells and lamina neurons. The belEY08943 mutant exhibits a less striking phenotype: a significant difference was observed in the PDF positive s-LNvs only in constant darkness, where the oscillation of PER is 4 h delayed compared to control, similarly to what described in belcap-1 flies. Both belle mutants are characterized by a reduction in the number of l-LNvs: a high percentage of brains, in fact, presented three neurons instead of the canonical four (83.93, 76.28, and 6.78% in bel cap-1, bel EY08943, and white 1118, respectively). In contrast, RNAi against belle in the photoreceptor cells (GMR-Gal4 and ninaE-Gal4) does not affect either vitality or behavior. Locomotor activity of belle knockdown flies under different conditions, overview
additional information
in order to increase the peptide linker region length, a 23 amino acid residue polypeptide with a composition of NASSGSSASSPSASNSPGANGSS was inserted between the native interdomain region's Ala and Thr residues. The sequence of the new extended interdomain linker is PANSSIANASSGSSASSPSASNSPGANGSSTLEAE. This peptide sequence is chosen because it has similar structural and dynamic properties to the native interdomain region, and both the designed and the native interdomain linker are predicted to form a flexible and unstructured region. In addition, since DbpA is purified as a native protein, small and polar amino acids, which promote peptide solubility, are placed into the polypeptide insert to discourage the aggregation of extended DbpA and its partition into inclusion bodies. The new interdomain linker is not digested by the Escherichia coli proteolytic enzymes and the extended DbpA is expressed as an intact and soluble protein. Breaking the sequence of the interdomain peptide linker and inserting the 23 amino acids peptide segment causes a decrease in binding affinity, likely as a consequence of formation of non-native interaction between the insert peptide and the RNA molecule or other regions of the protein and not a consequence of disrupting native interactions between the DbpA RNA binding domain and the interdomain linker. The peptide extension is not effecting the formation of the proper ATP pocket, but the ATP turnover rate is affected by the peptide extension. Although the ATP turnover of the extended DbpA is reduced when compared to wild-type DbpA, extended DbpA is a much more efficient enzyme than many members of DEAD-box family of proteins. The reduction on the ATP turnover of the extended DbpA is a consequence of its decrease in binding affinity for RNA. The extension of the interdomain linker region has no effect on the ability of DbpA to perform its helicase function. Thus, the physical connection of DbpA RNA binding domain to the catalytic core is unimportant for the helicase activity of DbpA, suggesting the DbpA protein is a region-specific enzyme, which would unwind any double-helix substrate near hairpin 92
additional information
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construction of the NS3-4A mutant affected in its acidic domain, the mutant shows altered RNA binding and increased ATPase activity, kinetics, overview
additional information
construction of the NS3-4A mutant affected in its acidic domain, the mutant shows altered RNA binding and increased ATPase activity, kinetics, overview
additional information
mutagenesis of conserved p54 helicase motifs activates translation in the tethered function assay, reduces accumulation of p54 in P-bodies in HeLa cells, and inhibits its capacity to assemble P-bodies in p54-depleted cells
additional information
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mutagenesis of conserved p54 helicase motifs activates translation in the tethered function assay, reduces accumulation of p54 in P-bodies in HeLa cells, and inhibits its capacity to assemble P-bodies in p54-depleted cells
additional information
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recombinant RHA domains are evaluated for binding activity to post-transcriptional control element (PCE) in comparison with nonfunctional PCE and generic control double-stranded RNAs (dsRNAs). N-terminal domain exhibits higher binding affinity for PCE than for nonfunctional mutant RNA or control dsRNA. Highly conserved surface-exposed lysine residues are required for selective interaction with PCE RNA. In cells, the N-terminal domain directs interaction with PCE, mRNA and its exogenous expression blocks the translation activity of endogenous RHA
additional information
enzyme inhibition by siRNA
additional information
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enzyme inhibition by siRNA
additional information
enzyme knockout using two DDX21 siRNAs
additional information
wild-type and mutant enzymes in vitro RNA binding and unwinding or in the cell during HIV-1 production during RNA helicase A-RNA interaction and RNA helicase A-stimulated viral RNA processes, overview. The mutations do not prevent RNA helicase A from binding to HIV-1 RNA in vitro aswell, but dramatically reduce RNA helicase A-HIV-1 RNA interaction in the cells
additional information
generation of codon-optimized DNA fragments encoding selected regions of hBrr2
additional information
generation of the DELTAUPF1_1x02loop and UPF1_1DELTACHx02loop mutants, and of truncation mutant UPF1_2DELTACH
additional information
isolation of the catalytically active helicase core DHX8DELTA547 enzyme fragment. The structure of DHX8DELTA547 reveals flexibility in the DEAH motif. The two DHX8DELTA547-ADP structures reveal a domain organisation very similar to that of other DEAH-box helicases. DHX8DELTA547 adopts a pyramidal-like structure with the two N-terminal RecA domains and the C-terminal ratchet-like and OB-fold domains on opposite sides of the putative DHX8 RNA-binding tunnel, and the C- and N-terminal domains connected by the WH domain. Comparison of kinetics of wild-type full-length enzyme and truncated mutant, overview
additional information
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isolation of the catalytically active helicase core DHX8DELTA547 enzyme fragment. The structure of DHX8DELTA547 reveals flexibility in the DEAH motif. The two DHX8DELTA547-ADP structures reveal a domain organisation very similar to that of other DEAH-box helicases. DHX8DELTA547 adopts a pyramidal-like structure with the two N-terminal RecA domains and the C-terminal ratchet-like and OB-fold domains on opposite sides of the putative DHX8 RNA-binding tunnel, and the C- and N-terminal domains connected by the WH domain. Comparison of kinetics of wild-type full-length enzyme and truncated mutant, overview
additional information
knockout of enzyme Lmo1722 decreases the number of mature 70S ribosomes at low temperatures and decreases Listeria monocytogenes motility by downregulating flaA expression
additional information
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knockout of enzyme Lmo1722 decreases the number of mature 70S ribosomes at low temperatures and decreases Listeria monocytogenes motility by downregulating flaA expression
additional information
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knockout of enzyme Lmo1722 decreases the number of mature 70S ribosomes at low temperatures and decreases Listeria monocytogenes motility by downregulating flaA expression
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additional information
trageting of the enzyme DDX6 with shRNA in N2a cells. Construction of a mutant DDX6 that contains a point mutation within the DEAD box motif II of DDX6 and thus lacks helicase activity, but is still able to coimmunoprecipitate TRIM32
additional information
generation of Ddx3xfl/fl mice, analysis of DDX3X and DDX3Y activity in fibroblasts from gene-targeted mice. Mouse embryonic fibroblasts (MEFs) derived from female Ddx3xfl/fl CreERT2 mice are treated with 4-OHT to delete Ddx3x. Innate immunity of DDX3X-deficient cells and of Ddx3xfl/y Vav-iCre mice is analyzed, overview. Mice lacking DDX3X in hematopoietic cells have reduced numbers of lymphocytes and natural killer cells. Mice lacking DDX3X in the hematopoietic system produce reduced amounts of serum IL-12 and IFNgamma after Listeria monocytogenes infection compromising the immune response of macrophages
additional information
plasmids and siRNAs are transfected in HEK-293T cells using calcium phosphate protocol. NIH 3T3 mouse fibroblasts, U2OS, and murine embryonic stem cells are transfected with the siRNA, siRNA-mediated depletions and synthetic RNA levels are monitored by quantitative RT-PCR expression analysis 3-4 days post transfection
additional information
construction of FRH truncated variants beginning at residue 100 or 114 (FRH-DELTA100 or FRHDELTA114)
additional information
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construction of FRH truncated variants beginning at residue 100 or 114 (FRH-DELTA100 or FRHDELTA114)
additional information
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construction of FRH truncated variants beginning at residue 100 or 114 (FRH-DELTA100 or FRHDELTA114)
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additional information
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construction of FRH truncated variants beginning at residue 100 or 114 (FRH-DELTA100 or FRHDELTA114)
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additional information
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construction of FRH truncated variants beginning at residue 100 or 114 (FRH-DELTA100 or FRHDELTA114)
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additional information
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construction of FRH truncated variants beginning at residue 100 or 114 (FRH-DELTA100 or FRHDELTA114)
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additional information
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construction of FRH truncated variants beginning at residue 100 or 114 (FRH-DELTA100 or FRHDELTA114)
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additional information
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the N-terminal part of the TGBp1 NTPase/helicase domain comprising conserved motifs I, Ia and II is sufficient for ATP hydrolysis, RNA binding and homologous proteinprotein interactions. Point mutations in a single conserved basic amino acid residue upstream of motif I have little effect on the activities of C-terminally truncated mutants of both TGBp1 proteins. When introduced into the full-length NTPase/helicase domains, these mutations cause a substantial decrease in the ATPase activity of the protein, suggesting that the conserved basic amino acid residue upstream of motif I is required to maintain a reaction-competent conformation of the TGBp1 ATPase active site
additional information
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the N-terminal part of the TGBp1 NTPase/helicase domain comprising conserved motifs I, Ia and II is sufficient for ATP hydrolysis, RNA binding and homologous proteinprotein interactions. Point mutations in a single conserved basic amino acid residue upstream of motif I have little effect on the activities of C-terminally truncated mutants of both TGBp1 proteins. When introduced into the full-length NTPase/helicase domains, these mutations cause a substantial decrease in the ATPase activity of the protein, suggesting that the conserved basic amino acid residue upstream of motif I is required to maintain a reaction-competent conformation of the TGBp1 ATPase active site
additional information
construction of an deletion mutant DELTAdeaD
additional information
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construction of an deletion mutant DELTAdeaD
additional information
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construction of an deletion mutant DELTAdeaD
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additional information
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construction of an deletion mutant DELTAdeaD
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additional information
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construction of an deletion mutant DELTAdeaD
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additional information
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construction of an deletion mutant DELTAdeaD
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additional information
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construction of an deletion mutant DELTAdeaD
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additional information
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construction of an deletion mutant DELTAdeaD
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additional information
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construction of an deletion mutant DELTAdeaD
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additional information
an NS3 mutant, that is deficient in RNA binding and its associated RSS activity, is inactive in complementing the RNA silencing suppressor function of the Tat protein of Human immunodeficiency virus type 1
additional information
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an NS3 mutant, that is deficient in RNA binding and its associated RSS activity, is inactive in complementing the RNA silencing suppressor function of the Tat protein of Human immunodeficiency virus type 1
additional information
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an NS3 mutant, that is deficient in RNA binding and its associated RSS activity, is inactive in complementing the RNA silencing suppressor function of the Tat protein of Human immunodeficiency virus type 1
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additional information
construction of PCR-generated truncated fragments of cshA, including the ATPase and the helicase domains and ending in a stop codon. Genes more abundant in the wild-type than in the cshA mutant upon MazFsa expression, overview. Mutation of cshA affects growth and cell viability
additional information
construction of PCR-generated truncated fragments of cshA, including the ATPase and the helicase domains and ending in a stop codon. Genes more abundant in the wild-type than in the cshA mutant upon MazFsa expression, overview. Mutation of cshA affects growth and cell viability
additional information
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construction of PCR-generated truncated fragments of cshA, including the ATPase and the helicase domains and ending in a stop codon. Genes more abundant in the wild-type than in the cshA mutant upon MazFsa expression, overview. Mutation of cshA affects growth and cell viability
additional information
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construction of PCR-generated truncated fragments of cshA, including the ATPase and the helicase domains and ending in a stop codon. Genes more abundant in the wild-type than in the cshA mutant upon MazFsa expression, overview. Mutation of cshA affects growth and cell viability
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additional information
Thermochaetoides thermophila
design of a mutant of Prp43 which allows us to trap the closed conformation by the introduction of an internal disulfide bond (ctPrp43-IDSB). For this purpose, one cysteine is introduced into the RecA1 domain and another one into the ratchet-like domain at exposed positions to maximize the number of formed disulfide bonds. The wild-type protein contains nine cysteines, the ctPrp43-IDSB mutant two additional ones, the majority of ctPrp43-IDSB exhibits the internal disulfide bridge. Prp43 trapped in the closed conformation is impaired in its helicase activity. The intrinsic ATPase activity of ctPrp43-IDSB is similar to the one determined for wild-type ctPrp43. ctPrp43-IDSB is also stimulated by ctPfa1-GP and by U16-RNA in the presence of the ctPfa1-GP, but in the contrast to wild-type Prp43 also just by U16-RNA. Prp43 in the trapped closed conformation appears to be more prone for the stimulation of the ATPase. Conformational rearrangements at the helicase core, structure analysis, overview
additional information
Thermochaetoides thermophila CBS 144.50
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design of a mutant of Prp43 which allows us to trap the closed conformation by the introduction of an internal disulfide bond (ctPrp43-IDSB). For this purpose, one cysteine is introduced into the RecA1 domain and another one into the ratchet-like domain at exposed positions to maximize the number of formed disulfide bonds. The wild-type protein contains nine cysteines, the ctPrp43-IDSB mutant two additional ones, the majority of ctPrp43-IDSB exhibits the internal disulfide bridge. Prp43 trapped in the closed conformation is impaired in its helicase activity. The intrinsic ATPase activity of ctPrp43-IDSB is similar to the one determined for wild-type ctPrp43. ctPrp43-IDSB is also stimulated by ctPfa1-GP and by U16-RNA in the presence of the ctPfa1-GP, but in the contrast to wild-type Prp43 also just by U16-RNA. Prp43 in the trapped closed conformation appears to be more prone for the stimulation of the ATPase. Conformational rearrangements at the helicase core, structure analysis, overview
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additional information
Thermochaetoides thermophila DSM 1495
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design of a mutant of Prp43 which allows us to trap the closed conformation by the introduction of an internal disulfide bond (ctPrp43-IDSB). For this purpose, one cysteine is introduced into the RecA1 domain and another one into the ratchet-like domain at exposed positions to maximize the number of formed disulfide bonds. The wild-type protein contains nine cysteines, the ctPrp43-IDSB mutant two additional ones, the majority of ctPrp43-IDSB exhibits the internal disulfide bridge. Prp43 trapped in the closed conformation is impaired in its helicase activity. The intrinsic ATPase activity of ctPrp43-IDSB is similar to the one determined for wild-type ctPrp43. ctPrp43-IDSB is also stimulated by ctPfa1-GP and by U16-RNA in the presence of the ctPfa1-GP, but in the contrast to wild-type Prp43 also just by U16-RNA. Prp43 in the trapped closed conformation appears to be more prone for the stimulation of the ATPase. Conformational rearrangements at the helicase core, structure analysis, overview
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additional information
Thermochaetoides thermophila IMI 039719
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design of a mutant of Prp43 which allows us to trap the closed conformation by the introduction of an internal disulfide bond (ctPrp43-IDSB). For this purpose, one cysteine is introduced into the RecA1 domain and another one into the ratchet-like domain at exposed positions to maximize the number of formed disulfide bonds. The wild-type protein contains nine cysteines, the ctPrp43-IDSB mutant two additional ones, the majority of ctPrp43-IDSB exhibits the internal disulfide bridge. Prp43 trapped in the closed conformation is impaired in its helicase activity. The intrinsic ATPase activity of ctPrp43-IDSB is similar to the one determined for wild-type ctPrp43. ctPrp43-IDSB is also stimulated by ctPfa1-GP and by U16-RNA in the presence of the ctPfa1-GP, but in the contrast to wild-type Prp43 also just by U16-RNA. Prp43 in the trapped closed conformation appears to be more prone for the stimulation of the ATPase. Conformational rearrangements at the helicase core, structure analysis, overview
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