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Information on EC 2.7.7.52 - RNA uridylyltransferase
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2.7.7.52 RNA uridylyltransferaseIUBMB Comments
The enzyme requires an oligoribonucleotide or polyribonucleotide with a free terminal 3'-OH as a primer.
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The enzyme appears in viruses and cellular organisms
Synonyms
tailor, tutase, zcchc11, terminal uridylyl transferase, heso1, rna editing tutase, terminal uridylyltransferase, meat1, tutase 1, u6-tutase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3' terminal uridylyl transferase
At2g45620
caffeine-induced death suppressor protein 1
Cid1
HESO1
RET1
Tailor
TbMP57 TUTase
terminal RNA uridylyltransferase
terminal U transferase (TUTase)
terminal uridylyl transferase
terminal uridylyltransferase
TUT
-
-
-
-
TUT1
TUT4
TUT7
TUTase
TUTase4
TUTase6
TUTase7
uridylyltransferase, terminal
-
-
-
-
URT1
Zcchc11
ZCCHC6
additional information
terminal uridylyltransferase
-
-
-
-
additional information
-
enzyme is a member of the DNA polymerase beta nucleotidyltransferase superfamily
additional information
-
the enzyme belongs to a large enzyme superfamily typified by DNA polymerase beta
additional information
-
enzyme is a member of the DNA polymerase beta nucleotidyltransferase superfamily
additional information
-
the enzyme belongs to a large enzyme superfamily typified by DNA polymerase beta
additional information
the enzyme belongs to a large enzyme superfamily typified by DNA polymerase beta
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UTP + RNAn = diphosphate + RNAn+3'-U
mechanism, uridine insertion in the editing process
-
UTP + RNAn = diphosphate + RNAn+3'-U
enzyme requires an oligoribonucleotide or polyribonucleotide with a free terminal 3'-OH as a primer
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
UTP:RNA uridylyltransferase
The enzyme requires an oligoribonucleotide or polyribonucleotide with a free terminal 3'-OH as a primer.
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CAS REGISTRY NUMBER
COMMENTARY
78519-53-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 5'(ppp)-UGAGGUAGUAGGUUGUAUAGUU-3'
diphosphate + 5'(ppp)-UGAGGUAGUAGGUUGUAUAGUUA-3'
-
i.e. triphosphorylated human let-7a-5p-3p
-
-
?
ATP + 5'-UGAGGUAGUAGGUUGUAUAGUU-3'
diphosphate + 5'-UGAGGUAGUAGGUUGUAUAGUUA-3'
-
i.e. unphosphorylated human let-7a-0P. Gld2 displays an 83fold preference of ATP over UTP
-
-
?
ATP + U6 small nuclear RNA
?
isoform TUT1 incorporates UMP more efficiently than AMP into U6 small nuclear RNA transcript ending with four uridines
-
-
?
CTP + 5'(pp)-UGAGGUAGUAGGUUGUAUAGUU-3'
diphosphate + 5'(pp)-UGAGGUAGUAGGUUGUAUAGUUC-3'
-
i.e. diphosphorylated human let-7a-5p-2p
-
-
?
UTP + 5'(p)-UGAGGUAGUAGGUUGUAUAGUU-3'
diphosphate + 5'(p)-UGAGGUAGUAGGUUGUAUAGUUU-3'
-
i.e. monophosphorylated human let-7a-5p. Gld2 displays an 83fold preference of ATP over UTP
-
-
?
UTP + miR-1003-3p-G
?
22-nt single stranded RNA oligonucleotide derived from the miR-1003 stem-loop
-
-
?
UTP + miR158an
diphosphate + miR158an+1
miR158a has the sequence 5'-Cy5-UCCCAAAUGUAGACAAAGCA-3'
-
-
?
UTP + mirtronRNAn
diphosphate + mirtronRNAn+1
the enzyme preferentially catalyzes the uridylation of mirtronRNAs ending in 3'G and 3'U
-
-
?
UTP + precursor let-7 RNAn
diphosphate + precursor let-7 RNAn+1
the interaction between the Lin28:pre-let-7 complex and the N-terminal Lin28-interacting module of TUT4 is required for prelet-7 oligo-uridylylation by the C-terminal catalytic module of TUT4/7
-
-
?
UTP + precursor let-7a-1 RNAn
diphosphate + precursor let-7a-1 RNAn+1
-
-
-
?
UTP + RNAn containing a terminal G residue
diphosphate + RNAn+1
-
substrate dsRNA
-
-
?
UTP + U6 small nuclear RNA
?
isoform TUT1 incorporates UMP more efficiently than AMP into U6 small nuclear RNA transcript ending with four uridines
-
-
?
UTP + U6 snRNAn
diphosphate + U6 snRNAn+1
the enzyme builds or repairs the 3'-oligo-uridylylated tail of U6 snRNA
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
editosomal enzyme form, no activity
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
editosomal enzyme form, no activity
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
about 50% of the activity with UTP, prefers Mn2+ as divalent cation
-
-
?
GTP + RNAn
diphosphate + RNAn+1
-
editosomal enzyme form, no activity
-
-
?
UTP + miRNAn
diphosphate + miRNAn+1
the enzyme URT1 plays a redundant but important role in miRNA uridylation when HESO1 is absent
-
-
?
UTP + mRNAn
diphosphate + mRNAn+1
for mRNA, URT1 is the main enzyme to uridylate the majority of mRNA and repairs their deadenylated ends to restore the binding site for poly(A) binding protein. Enzyme HESO1, on the other hand, targets mostly the mRNAs with very short oligo(A) tails and fails in fulfilling the same task
-
-
?
UTP + mRNAn
diphosphate + mRNAn+1
for mRNA, URT1 is the main enzyme to uridylate the majority of mRNA (70-80%) and repairs their deadenylated ends to restore the binding site for poly(A) binding protein. Enzyme HESO1, on the other hand, targets mostly the mRNAs with very short oligo(A) tails and fails in fulfilling the same task
-
-
?
UTP + poly(A) tail mimic RNAn
diphosphate + poly(A) tail mimic RNAn+1
-
-
-
-
?
UTP + poly(A) tail mimic RNAn
diphosphate + poly(A) tail mimic RNAn+1
Schizosaccharomyces pombe BG 0000H6
-
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
small guide RNA, i.e. gRNA
-
?
UTP + RNAn
diphosphate + RNAn+1
-
marked specificity for UTP
-
?
UTP + RNAn
diphosphate + RNAn+1
-
responsible for post-transcriptional RNA editing process of mitochondrial transcripts in kinetoplastid protozoans
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of non-coded poly(U) tail to gRNAs
-
?
UTP + RNAn
diphosphate + RNAn+1
-
enzyme preferentially uridylates mirtron hairpins
-
?
UTP + RNAn
diphosphate + RNAn+1
the enzyme exhibits an intrinsic preference for RNA substrates ending in 3'G
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
specifically modifies the 3'-UMP terminal of mammalian U6 small nuclear RNA, i.e. snRNA, structural requirements and specificity, overview
-
?
UTP + RNAn
diphosphate + RNAn+1
-
acts as a host factor to initiate RNA synthesis by poliovirus RNA polymerase in vitro
-
?
UTP + RNAn
diphosphate + RNAn+1
the enzyme mediates template-independent uridylylation at the 3'-end of RNAs
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
RNA substrate specificity, overview
-
?
UTP + RNAn
diphosphate + RNAn+1
-
editosomal enzyme form shows preference for a 3' terminal A or G, while the mitochondrial enzyme form does not
-
?
UTP + RNAn
diphosphate + RNAn+1
-
mitochondrial enzyme form adds Us at the 3' and the 5' end of the RNA
-
?
UTP + RNAn
diphosphate + RNAn+1
-
the mitochondrial enzyme adds a single U to the 3'-end of single-stranded RNA
-
?
UTP + RNAn
diphosphate + RNAn+1
-
involved in uridine insertion in the editing process of RNA
-
?
UTP + RNAn
diphosphate + RNAn+1
-
responsible for post-transcriptional RNA editing process of mitochondrial transcripts in kinetoplastid protozoans
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of non-coded poly(U) tail to gRNAs
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of non-coded poly(U) tail to gRNAs
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of primarily single U to single-stranded RNA, addition of the number of Us specified by a guide RNA to insertion editing-like substrates
-
?
UTP + RNAn
diphosphate + RNAn+1
-
TbMP57 TUTase, an enzyme thought to act exclusively in U-insertion, can also function within the U-deletion cycle, after cleavage and 3'-U-exo but before U-deletional cycle
-
-
?
UTP + RNAn
diphosphate + RNAn+1
a template-independent RNA nucleotidyltransferases that specifically recognize UTP, it possesses conserved catalytic and UTP recognition domains. A single nucleoside triphosphate is bound in the active site by a complex network of interactions between amino acid residues, a magnesium ion and highly ordered water molecules with the UTPs base, ribose and phosphate moieties, structure-function analysis, overview
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
invariant arginine residues 144 and 435 positioned in the vicinity of the UTP-binding site are critical for isoform RET2 activity on single-stranded and double-stranded RNAs, as well as function in vivo. Recognition of a double-stranded RNA, which resembles a guide RNA/mRNA duplex, is further facilitated by multipoint contacts across the RET2-specific middle domain
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
TbMP57 TUTase, an enzyme thought to act exclusively in U-insertion, can also function within the U-deletion cycle, after cleavage and 3'-U-exo but before U-deletional cycle
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
the enzyme requires a single-stranded oligoribonucleotide or polyribonucleotide with a free terminal 3'-OH as primer, e.g. oligoA20, tRNAAsp, E. coli RNA, alfalafa mosaic virus RNA 4
-
?
UTP + RNAn
diphosphate + RNAn+1
-
RNA substrate specificity, overview
-
?
UTP + RNAn
diphosphate + RNAn+1
-
RNA uridylyltransferase might function in uridylating specific proteins, RNA is not a natural substrate
-
?
UTP + RNAn containing a terminal U residue
diphosphate + RNAn+1
-
substrate dsRNA
-
-
?
additional information
?
-
enzyme shows strong preference for uridine and a distributive activity for the first added nucleotides. URT1 uridylates oligoadenylated mRNAs
-
-
?
additional information
?
-
HESO1 exhibits nucleotidyl transferase activity on methylated miRNA in vitro. HESO1 has a clear preference for miR158A-U. miR158A-G is the second most preferred substrate
-
-
?
additional information
?
-
HESO1 exhibits nucleotidyl transferase activity on methylated miRNA in vitro. HESO1 has a clear preference for miR158A-U. miR158A-G is the second most preferred substrate
-
-
?
additional information
?
-
URT1 exhibits nucleotidyl transferase activity on unmethylated miRNA in vitro. URT1 shows a strong preference for miR158 ending in A, miR158A-C, miR158A-G, and miR158A-U are similarly used by URT1
-
-
?
additional information
?
-
URT1 exhibits nucleotidyl transferase activity on unmethylated miRNA in vitro. URT1 shows a strong preference for miR158 ending in A, miR158A-C, miR158A-G, and miR158A-U are similarly used by URT1
-
-
?
additional information
?
-
enzyme shows strong preference for uridine and a distributive activity for the first added nucleotides. URT1 uridylates oligoadenylated mRNAs
-
-
?
additional information
?
-
the enzyme exhibits significantly higher tailing efficiency for substrates with a 3'-terminal G or U
-
-
-
additional information
?
-
-
human Gld2 is a bona fide adenylyltransferase with only weak activity toward other nucleotides. Gld2 is a promiscuous enzyme, with activity toward miRNA, pre-miRNA, and polyadenylated RNA substrates. Gld2 shows a clear preference for ATP in the presence of all four NTPs. Apo-Gld2 activity is restricted to adding single nucleotides and processivity likely relies on additional RNA-binding proteins
-
-
?
additional information
?
-
-
enzyme interacts with a minor fraction of total RNA ligase
-
-
?
additional information
?
-
-
post-transcriptional uridylylation of guide RNAs by RNA editing TUTase 1 or RET1, a multi-functional RNA processing enzyme, and U-insertion mRNA editing by RNA editing TUTase 2 or RET2, biological functions of TUT isozymes, RNA processing in mitochondria of trypanosomes, detailed overview
-
-
?
additional information
?
-
-
UTP recognition mechanism, overview. The NTD-CTD bi-domain catalytic modules shared by TUTases and non-canonical poly(A) polymerases, ncPAPs, are quite promiscuous in NTP binding, NTP selectivity of TUTase-like catalytic modules, RNA specificity, overview
-
-
?
additional information
?
-
-
reduction of isozyme RET1 leads to decrease in edited RNA and inhibited growth, lowers the uridine insertion and leads predominantly to shorter gRNAs
-
-
?
additional information
?
-
-
down-regulation of isozyme RET2 inhibits growth and in vivo uridine insertion, but has no effect on the length of gRNAs
-
-
?
additional information
?
-
-
many editing changes are developmentally regulated
-
-
?
additional information
?
-
-
down-regulation of RET1, but not of RET2, affects length distribution of gRNA 3' oligo(U) tails
-
-
?
additional information
?
-
-
Inhibition of RNA editing by down-regulation of expression of the mitochondrial RNA editing TUTase 1 by RNA interference has profound effects on kinetoplast biogenesis in Trypanosoma brucei procyclic cells. De novo synthesis of the apocytochrome b and cytochrome oxidase subunit I proteins is no longer detectable after 3 days of RNAi. The effect on protein synthesis correlates with a decline in the levels of the assembled mitochondrial respiratory complexes III and IV, and also with cyanide-sensitive oxygen uptake. The steady-state levels of nuclear-encoded subunits of complexes III and IV are also significantly decreased. Because the levels of the corresponding mRNAs are not affected, the observed effect is likely due to an increased turnover of these imported mitochondrial proteins. This induced protein degradation is selective for components of complexes III and IV, because little effect is observed on components of the F1-F0 -ATPase complex and on several other mitochondrial proteins
-
-
?
additional information
?
-
-
post-transcriptional uridylylation of guide RNAs by RNA editing TUTase 1 or RET1, a multi-functional RNA processing enzyme, and U-insertion mRNA editing by RNA editing TUTase 2 or RET2, biological functions of TUT isozymes, RNA processing in mitochondria of trypanosomes, detailed overview
-
-
?
additional information
?
-
TUT4 substrate specificity toward nucleoside triphosphate substrates with a synthetic 5'-radiolabeled 24-mer RNA as a primer, in presence of Mg2+ ions TUT4 preferentially incorporates uridylyl residues but the reaction with CTP is also detectable, TbTUT4 incorporates only one deoxynucleotide into RNA, overview. UTP binding site structure and structure-activity analysis
-
-
?
additional information
?
-
-
UTP recognition mechanism, overview. UTP specificity is determined primarily by the two closely positioned carboxylic residues, D297/D421 and E300/E424, which coordinate a crucial water molecule indicated in TUT4/RET2, uracil base interactions with invariant amino acids N147, S148, Y189, D297, E300 of TUT4. The NTD-CTD bi-domain catalytic modules shared by TUTases and non-canonical poly(A) polymerases, ncPAPs, are quite promiscuous in NTP binding, NTP selectivity of TUTase-like catalytic modules, RNA specificity, overview
-
-
?
additional information
?
-
-
isoform RET1 adds U tails to gRNAs, rRNAs, and selected mRNAs and contributes U residues into A/U heteropolymers. Isoform RET1's terminal uridylyl transferase activity is required for the nucleolytic processing of gRNA, rRNA, and mRNA precursors. The U tails presence does not affect the stability of gRNAs and rRNAs, while transcript-specific uridylylation triggers 3' to 5' mRNA decay. The minicircle-encoded antisense transcripts, which are stabilized by RET1-catalyzed uridylylation, may direct a nucleolytic cleavage of multicistronic precursors
-
-
?
additional information
?
-
-
recombinant RET2 catalyzes a faithful editing on gapped precleaved double-stranded RNA substrates, and this reaction requires an internal monophosphate group at the 5' end of the mRNA 3' cleavage fragment. RET2 processivity is limited to insertion of three U residues. Incorporation into the RNA editing core complex RECC allows filling of longer gaps similar to those observed in vivo. Monomeric and RECC-embedded enzymes display a similar bimodal activity, the distributive insertion of a single uracil is followed by a processive extension limited by the number of guiding nucleotides. The distributive +1 insertion creates a substrate for the processive gap-filling reaction. Upon base-pairing of the +1 extended 5' cleavage fragment with a guiding nucleotide, this substrate is recognized by RET2 in a different mode compared to the product of the initial nucleolytic cleavage. Therefore, RET2 distinguishes base pairs in gapped RNA substrates
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UTP + precursor let-7 RNAn
diphosphate + precursor let-7 RNAn+1
the interaction between the Lin28:pre-let-7 complex and the N-terminal Lin28-interacting module of TUT4 is required for prelet-7 oligo-uridylylation by the C-terminal catalytic module of TUT4/7
-
-
?
UTP + U6 snRNAn
diphosphate + U6 snRNAn+1
the enzyme builds or repairs the 3'-oligo-uridylylated tail of U6 snRNA
-
-
?
UTP + mRNAn
diphosphate + mRNAn+1
for mRNA, URT1 is the main enzyme to uridylate the majority of mRNA and repairs their deadenylated ends to restore the binding site for poly(A) binding protein. Enzyme HESO1, on the other hand, targets mostly the mRNAs with very short oligo(A) tails and fails in fulfilling the same task
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
responsible for post-transcriptional RNA editing process of mitochondrial transcripts in kinetoplastid protozoans
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of non-coded poly(U) tail to gRNAs
-
?
UTP + RNAn
diphosphate + RNAn+1
the enzyme exhibits an intrinsic preference for RNA substrates ending in 3'G
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
acts as a host factor to initiate RNA synthesis by poliovirus RNA polymerase in vitro
-
?
UTP + RNAn
diphosphate + RNAn+1
the enzyme mediates template-independent uridylylation at the 3'-end of RNAs
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
involved in uridine insertion in the editing process of RNA
-
?
UTP + RNAn
diphosphate + RNAn+1
-
responsible for post-transcriptional RNA editing process of mitochondrial transcripts in kinetoplastid protozoans
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of non-coded poly(U) tail to gRNAs
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of non-coded poly(U) tail to gRNAs
-
?
UTP + RNAn
diphosphate + RNAn+1
-
addition of primarily single U to single-stranded RNA, addition of the number of Us specified by a guide RNA to insertion editing-like substrates
-
?
UTP + RNAn
diphosphate + RNAn+1
-
RNA uridylyltransferase might function in uridylating specific proteins, RNA is not a natural substrate
-
?
additional information
?
-
-
enzyme interacts with a minor fraction of total RNA ligase
-
-
?
additional information
?
-
-
post-transcriptional uridylylation of guide RNAs by RNA editing TUTase 1 or RET1, a multi-functional RNA processing enzyme, and U-insertion mRNA editing by RNA editing TUTase 2 or RET2, biological functions of TUT isozymes, RNA processing in mitochondria of trypanosomes, detailed overview
-
-
?
additional information
?
-
-
reduction of isozyme RET1 leads to decrease in edited RNA and inhibited growth, lowers the uridine insertion and leads predominantly to shorter gRNAs
-
-
?
additional information
?
-
-
down-regulation of isozyme RET2 inhibits growth and in vivo uridine insertion, but has no effect on the length of gRNAs
-
-
?
additional information
?
-
-
many editing changes are developmentally regulated
-
-
?
additional information
?
-
-
down-regulation of RET1, but not of RET2, affects length distribution of gRNA 3' oligo(U) tails
-
-
?
additional information
?
-
-
Inhibition of RNA editing by down-regulation of expression of the mitochondrial RNA editing TUTase 1 by RNA interference has profound effects on kinetoplast biogenesis in Trypanosoma brucei procyclic cells. De novo synthesis of the apocytochrome b and cytochrome oxidase subunit I proteins is no longer detectable after 3 days of RNAi. The effect on protein synthesis correlates with a decline in the levels of the assembled mitochondrial respiratory complexes III and IV, and also with cyanide-sensitive oxygen uptake. The steady-state levels of nuclear-encoded subunits of complexes III and IV are also significantly decreased. Because the levels of the corresponding mRNAs are not affected, the observed effect is likely due to an increased turnover of these imported mitochondrial proteins. This induced protein degradation is selective for components of complexes III and IV, because little effect is observed on components of the F1-F0 -ATPase complex and on several other mitochondrial proteins
-
-
?
additional information
?
-
-
post-transcriptional uridylylation of guide RNAs by RNA editing TUTase 1 or RET1, a multi-functional RNA processing enzyme, and U-insertion mRNA editing by RNA editing TUTase 2 or RET2, biological functions of TUT isozymes, RNA processing in mitochondria of trypanosomes, detailed overview
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mg2+
increases the UTP substrate specificity of TUT4 and influences the enzyme conformation
Mg2+
-
divalent cation required, Mg2+ or Mn2+, 4-12 mM stimulate, optimal at 5 mM
Mn2+
-
when GTP, CTP, or ATP are used as substrates, Mn2+ is more effective than Mg2+
Mn2+
replacement of magnesium with manganese leads to a dramatic stimulation of processivity and partial loss of selectivity for UTP
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ionic strength
-
quite sensitive to ionic strength, activity decreases by 50% at about 40 mM (NH4)2SO4 or 125 mM potassium acetate
-
additional information
-
RNA interference, i.e. RNAi, induced by tetracyclines causes down-regulation of RET1 and RET2 expression in vitro and in vivo
-
additional information
-
RNA interference, i.e. RNAi, induced by tetracyclines causes down-regulation of RET1 and RET2 expression in vitro and in vivo
-
additional information
-
not inhibitory: actinomycin C, rifamycin, alpha-amanitin, phosphate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
protein TbMP81
-
editosome protein, interaction enhances the enzyme activity
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state enzyme kinetics, overview
-
0.0004
RNAn
-
RNA editing core complex RECC, pH 8.0, temperature not specified in the publication
0.0025
RNAn
-
recombinant enzyme, pH 8.0, temperature not specified in the publication
0.0126
RNAn containing a terminal U residue
-
recombinant enzyme, pH 8.0, temperature not specified in the publication
-
0.0208
RNAn containing a terminal U residue
-
RNA editing core complex RECC, pH 8.0, temperature not specified in the publication
-
0.0005
UTP
-
mutant V271R/C83F, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.0006
UTP
-
mutant C83F, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.0025
UTP
-
wild-type, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.0026
UTP
-
mutant C83F, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.0028
UTP
-
mutant V271R, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.003
UTP
-
mutant V271R/C83F, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.0081
UTP
-
mutant K149A, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.0126
UTP
-
wild-type, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.0209
UTP
-
mutant V271R, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0003
RNAn
-
recombinant enzyme, pH 8.0, temperature not specified in the publication
0.0007
RNAn
-
RNA editing core complex RECC, pH 8.0, temperature not specified in the publication
0.0015
RNAn containing a terminal U residue
-
RNA editing core complex RECC, pH 8.0, temperature not specified in the publication
-
0.0033
RNAn containing a terminal U residue
-
recombinant enzyme, pH 8.0, temperature not specified in the publication
-
0.00002
UTP
-
mutant K149A, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.00003
UTP
-
mutant V271R, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.00005
UTP
-
mutant C83F, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.00012
UTP
-
mutant V271R/C83F, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.0003
UTP
-
wild-type, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.0012
UTP
-
mutant V271R, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.0015
UTP
-
mutant C83F, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.0018
UTP
-
mutant V271R/C83F, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.003
UTP
-
wild-type, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.133
RNAn
-
recombinant enzyme, pH 8.0, temperature not specified in the publication
0.167
RNAn
-
RNA editing core complex RECC, pH 8.0, temperature not specified in the publication
0.067
RNAn containing a terminal U residue
-
RNA editing core complex RECC, pH 8.0, temperature not specified in the publication
-
0.267
RNAn containing a terminal U residue
-
recombinant enzyme, pH 8.0, temperature not specified in the publication
-
0.0053
UTP
-
mutant K149A, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.0058
UTP
-
mutant V271R, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.0097
UTP
-
mutant V271R, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.0567
UTP
-
mutant C83F, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.0867
UTP
-
mutant C83F, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.117
UTP
-
wild-type, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.21
UTP
-
mutant V271R/C83F, cosubstrate RNAn containing a terminal G residue, pH 8.0, temperature not specified in the publication
0.25
UTP
-
wild-type, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
0.6
UTP
-
mutant V271R/C83F, cosubstrate RNAn containing a terminal U residue, pH 8.0, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.9
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
editosome protein TbMP57, distinct from mitochondrial enzyme form, i.e. TbTUTase 108
-
-
brenda
RET1 and RET2, i.e. RNA editing TUTases 1 and 2, as components of different editing complexes
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
2 isozymes RET1 and RET2 in mitochondria editosomes
brenda
additional information
-
isozymes are located in 2 different complexes
-
brenda
additional information
-
integral editosome protein, distinct from mitochondrial enzyme form
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
enzyme deletion increases sensitivity to protein misfolding stress
malfunction
Schizosaccharomyces pombe BG 0000H6
-
enzyme deletion increases sensitivity to protein misfolding stress
-
metabolism
isoform TUT1 catalyzes oligo-uridylylation of U6 small nuclear RNA, which catalyzes mRNA splicing. Oligo-uridylylation of U6 snRNA is required for U6 snRNA maturation, U4/U6-di-snRNP formation, and U6 snRNA recycling during mRNA splicing
metabolism
isoform TUT4 catalyzes mono- or oligo-uridylylation of precursor let-7 (pre-let-7). Let-7 RNA is broadly expressed in somatic cells and regulates cellular proliferation and differentiation. Mono-uridylylation of pre-let-7 by TUT4 promotes subsequent Dicer processing to up-regulate let-7 biogenesis
metabolism
isoform TUT7 catalyzes mono- or oligo-uridylylation of precursor let-7 (pre-let-7). Let-7 RNA is broadly expressed in somatic cells and regulates cellular proliferation and differentiation. Mono-uridylylation of pre-let-7 by TUT7 promotes subsequent Dicer processing to up-regulate let-7 biogenesis
metabolism
the enzyme plays a crucial role as the repressor in the biogenesis pathway of splicing-derived mirtron pre-miRNAs
metabolism
-
the enzyme uridylates polyadenylated mRNAs to trigger Lsm1-7-mediated decapping of the RNA 5'-end and subsequent degradation by the U-specific exonuclease Dis3L2
metabolism
the U6 snRNA-specific terminal uridylyltransferase is required for pre-mRNA splicing
metabolism
Schizosaccharomyces pombe BG 0000H6
-
the enzyme uridylates polyadenylated mRNAs to trigger Lsm1-7-mediated decapping of the RNA 5'-end and subsequent degradation by the U-specific exonuclease Dis3L2
-
physiological function
-
isoform RET1 adds U tails to gRNAs, rRNAs, and selected mRNAs and contributes U residues into A/U heteropolymers. Isoform RET1's terminal uridylyl transferase activity is required for the nucleolytic processing of gRNA, rRNA, and mRNA precursors. The U tails presence does not affect the stability of gRNAs and rRNAs, while transcript-specific uridylylation triggers 3' to 5' mRNA decay. The minicircle-encoded antisense transcripts, which are stabilized by RET1-catalyzed uridylylation, may direct a nucleolytic cleavage of multicistronic precursors
physiological function
-
isoform RET2 is an integral component of the RNA editing core complex RECC. Interaction of RET2 with RECC is accomplished via a protein-protein contact between its middle domain and structural subunit MP81. The recombinant RET2 catalyzes a faithful editing on gapped precleaved double-stranded RNA substrates, and this reaction requires an internal monophosphate group at the 5' end of the mRNA 3' cleavage fragment. RET2 processivity is limited to insertion of three U residues. Incorporation into the RECC voids the internal phosphate requirement and allows filling of longer gaps similar to those observed in vivo. Monomeric and RECC-embedded enzymes display a similar bimodal activity, the distributive insertion of a single uracil is followed by a processive extension limited by the number of guiding nucleotides
physiological function
isoform Rsp1 associates with uridylyltransferase Rdn1-RNA-dependent RNA polymerase Rdf1 or Rdn1-Rdf2 subcomplexes, creating Rsp1 complexes RSPCs that are physically separate from RNA-dependent RNA polymerase complexes RDRCs. The uridylyltransferase activity of Rdn1 is greatly reduced in RSPCs compared with RDRCs, suggesting enzyme regulation by the alternative partners. Despite the loss of all known RDRC-generated classes of endogenous sRNAs, RSP1 gene knockout is tolerated in growing cells. A minority class of dicer protein Dcr2-dependent sRNAs persists in cells lacking Rsp1 with increased size heterogeneity
physiological function
isoforms TUT7/ZCCHC6, TUT4/ZCCHC11, and TUT2/PAPD4/GLD2 are the terminal uridylyltransferases responsible for pre-miRNA mono-uridylation. The terminal uridylyl transferases act specifically on dsRNAs with a 1 nucleotide 3' overhang, thereby creating a 2 nucleotide 3' overhang. Depletion of terminal uridylyl transferases reduces let-7 microRNA levels and disrupts let-7 function. Although the let-7 suppressor, Lin28, induces inhibitory oligo-uridylation in embryonic stem cells, mono-uridylation occurs in somatic cells lacking Lin28 to promote let-7 biogenesis
physiological function
isoforms Zcchc11 and Zcchc6 redundantly control let-7 biogenesis in embryonic stem cells
physiological function
isoform HESO1, which uridylates most unmethylated miRNAs in vivo, and isoform URT1 which exhibits nucleotidyl transferase activity on unmethylated miRNA, prefer substrates with different 3'-end nucleotides in vitro and act cooperatively to tail different forms of the same miRNAs in vivo. Both HESO1 and URT1 exhibit nucleotidyl transferase activity on AGO1-bound miRNAs. Although the enzymes are able to add long tails to AGO1-bound miRNAs, the tailed miRNAs remain associated with AGO1. Tailing of AGO1-bound miRNA165/6 drastically reduces the slicing activity of AGO1-miR165/6
physiological function
isoform Tailor preferentially uridylates mirtron hairpins, thereby impeding the production of non-canonical microRNAs. Mirtron selectivity is explained by primary sequence specificity of Tailor, selecting substrates ending with a 3'-guanosine. In contrast to mirtrons, conserved Drosophila precursor micro-RNAs are significantly depleted in 3'-guanosine, thereby escaping regulatory uridylation. Cytoplasmic Tailor is required for miRNA uridylation and normal fertility in flies
physiological function
oligo(A)-tailed mRNAs are uridylated by the cytosolic UTP:RNA uridylyltransferase URT1, and URT1 has no major impact on mRNA degradation rates. In absence of uridylation, oligo(A) tails are trimmed, indicating that uridylation protects oligoadenylated mRNAs from 3'-ribonucleolytic attacks. URT1 mutants display an increase in 3'-truncated transcripts
physiological function
URT1 is the single most predominant nucleotidyl transferase that tails miRNAs. URT1 and isoform HESO1, which uridylates most unmethylated miRNAs in vivo, prefer substrates with different 3'-end nucleotides in vitro and act cooperatively to tail different forms of the same miRNAs in vivo. Both HESO1 and URT1 exhibit nucleotidyl transferase activity on AGO1-bound miRNAs. Although the enzymes are able to add long tails to AGO1-bound miRNAs, the tailed miRNAs remain associated with AGO1. Tailing of AGO1-bound miRNA165/6 drastically reduces the slicing activity of AGO1-miR165/6. Monouridylation of miR171a by URT1 endows the miRNA the ability to trigger the biogenesis of secondary siRNAs
physiological function
isoform TUT4 uridylates pre-miR-324, resulting in alternative processing by DICER. The altered cleavage leads to selection of the 3p strand instead of the 5p strand. Perturbation of the miR-324 arm usage disrupts glioblastoma cell proliferation
physiological function
isoform TUT7 uridylates pre-miR-324, resulting in alternative processing by DICER. The altered cleavage leads to selection of the 3p strand instead of the 5p strand. Perturbation of the miR-324 arm usage disrupts glioblastoma cell proliferation
physiological function
-
oligo(A)-tailed mRNAs are uridylated by the cytosolic UTP:RNA uridylyltransferase URT1, and URT1 has no major impact on mRNA degradation rates. In absence of uridylation, oligo(A) tails are trimmed, indicating that uridylation protects oligoadenylated mRNAs from 3'-ribonucleolytic attacks. URT1 mutants display an increase in 3'-truncated transcripts
-
Show AA Sequence and Transmembrane Helices (515 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
500000
700000
-
RNA-stabilized higher complexed form, native PAGE and glycerol gradient sedimentation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
a single C2H2-type zinc finger domain of Zcchc11 is responsible for the functional interaction with pluripotency factor Lin28. Lin28 uses terminal uridylyltransferases Zcchc11 and Zcchc6 to control let-7 expression and has important implications for stem cell biology as well as cancer
additional information
a single C2H2-type zinc finger domain of Zcchc11 is responsible for the functional interaction with pluripotency factor Lin28. Lin28 uses terminal uridylyltransferases Zcchc11 and Zcchc6 to control let-7 expression and has important implications for stem cell biology as well as cancer
additional information
isoform Rsp1 associates with uridylyltransferase Rdn1-RNA-dependent RNA polymerase Rdf1 or Rdn1-Rdf2 subcomplexes, creating Rsp1 complexes RSPCs that are physically separate from RNA-dependent RNA polymerase complexes RDRCs. The uridylyltransferase activity of Rdn1 is greatly reduced in RSPCs compared with RDRCs, suggesting enzyme regulation by the alternative partners
additional information
-
in RET1, an extra 150 amino acid insertion constitutes a helix-rich domain essential for activity, the insertion is designated as middle domain, occurs at a conserved site within the catalytic domain and is found in RET1, RET2 and TUT3, but not in TUT4, analysis of Structural diversity of trypanosomal TUTases, overview
additional information
TbTUT4 represents a minimal catalytically active RNA uridylyltransferase consisting of only two domains that define the catalytic center at the bottom of the nucleoside triphosphate and RNA substrate binding cleft. The enzyme shows two significantly different conformations: one molecule is in a relatively open apo conformation, whereas the other displays a more compact TUTase-UTP complex, structure-function analysis, overview
additional information
-
isoform RET2 is an integral component of the RNA editing core complex RECC
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutant enzyme D547A, sitting drop vapor diffusion method, using 0.1 M HEPES, pH 7.5, 10% (w/v) PEG 6000 and 5% (w/v) 2-methyl-2,4-pentanediol
enzyme bound to uridine-5'-[(alpha,beta)-imido]triphosphate, hanging drop vapor diffusion method, using 20% (v/v) glycerol ethoxylate. Enzyme bound to GpU, sitting drop vapor diffusion method, using 30% (v/v) glycerol ethoxylate and 60 mM sodium malonate, pH 7.0. Enzyme bound to CACAGU, hanging drop vapor diffusion method, using 35% (v/v) glycerol ethoxylate and 75 mM sodium malonate, pH 7.0. Enzyme bound to U6 RNA, sitting drop vapor diffusion method, using 35% (v/v) glycerol ethoxylate and 90 mM sodium malonate, pH 7.0
enzyme residues 202-560 and enzyme in complex with RNA stretches 5 -AGU-3 and 5 -AGUU-3 , sitting drop vapor diffusion method, using 0.1 M Tris-HCl, pH 8.4, 50 mM NaCl, 0.2 M lithium sulfate monohydrate and 15% (w/v) PEG3350
apoenzyme and enzyme in complex with UTP or ATP, hanging drop vapor diffusion method, using 13-15% (w/v) PEG3350 as the precipitant
Lin28-interacting module of TUT4, sitting drop vapor diffusion method, using 100 mM HEPES-NaOH, pH 7.0, 20% (w/v) PEG3350, 3% (v/v) 2-methyl-2,4-pentanediol, 200mM ammonium citrate, and 3% (w/v) 1,5 diaminopentane dihydrochloride
purified recombinant N-terminally His-tagged TUT4, free or with bound 2'-deoxyribonucleoside, at a concentration of 10 mg/mL in 10 mM HEPES, pH 7.6, 70 mM KCl, 0.5 mM DTT, and in presence of 4 mM MgCl2 and 0.05 mM UTP, screening with commercial crystallization screens, vapor diffusion technique, 4°C, cryoprotection by 15% glycerol, X-ray diffraction structure determination and analysis at 2.0-2.4 A resolution
small plate-like co-crystals of purified recombinant N-terminally His-tagged TbTUT4 and UTP grow in 100 mM sodium cacodylate (pH 6.5), 200 mM calcium acetate, 18% (w/v) PEG-8000, crystal structure reveals two significantly different conformations of this TUTase:one molecule is in a relatively open apo confirmation, whereas the other displays a more compact TUTase-UTP complex
structure of apoenzyme and in complex with UTP, to 1.56 A and 1.95 A resolution, respectively. Enzyme possesses a bridging domain, which extends from the C-terminal domain and makes hydrophobic contacts with the N-terminal domain, thereby creating a cavity adjacent to the UTP-binding site. Enzyme shows no appreciable conformational change upon UTP binding and apparently does not require RNA substrate to select a cognate nucleoside triphosphate.
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H294A
the enzymatic activity of the mutant is reduced by about 61% as compared to the wild type enzyme
N347A
the uridylation efficiency of the mutant is reduced dramatically to about 7% when compared with that of wild type enzyme
Q519A
the activity of the mutant is reduced compared to the wild type enzyme. The mutant tails 3'-G, 3'-A and 3'-C substrates with comparable efficiencies
R295A
the enzymatic activity of the mutant is reduced by about 84% as compared to the wild type enzyme
R295K
the enzymatic activity of the mutant is reduced by about 80% as compared to the wild type enzyme
R327A
R327K
V328I
the mutation barely affects the enzyme's binding with RNA substrate and also exhibits a obvious reduction in uridylation efficiency as compared to the wild type enzyme
V328L
the mutation entirely abolishes the enzyme's catalytic activity for truncated miR-1003 bearing 3'G. The mutation barely affects the enzyme's binding with RNA substrate
V328R
the mutation entirely abolishes the enzyme's catalytic activity for truncated miR-1003 bearing 3'G. The mutation barely affects the enzyme's binding with RNA substrate
C306A/C309A
the mutant does not oligo-uridylylate pre-let-7a-1 RNA in the presence of Lin28A
H405A/K452A
the mutant shows reduced oligo-uridylylation of pre-let-7a-1 RNA in the presence of Lin28A compared to the wild type enzyme
K321A/K324A
the mutant shows severely reduced oligo-uridylylation of pre-let-7a-1 RNA in the presence of Lin28A compared to the wild type enzyme
K326A/R327A
the mutant shows severely reduced oligo-uridylylation of pre-let-7a-1 RNA in the presence of Lin28A compared to the wild type enzyme
K329A/K330A
the mutant shows strongly reduced oligo-uridylylation of pre-let-7a-1 RNA in the presence of Lin28A compared to the wild type enzyme
R669A/R670A
the mutant shows strongly reduced oligo-uridylylation of pre-let-7a-1 RNA in the presence of Lin28A compared to the wild type enzyme
R779A/R783A
the mutations reduce the RNA-binding and uridylylation activities of the enzyme
R121A
Km=0.0028 (UTP), kcat=0.000033/sec (UTP),Km=0.132 (RNA), kcat= 0.005/sec (RNA)
R141A
R307A
Km=0.0004 (UTP), kcat=0.000133/sec (UTP), Km=0.01 (RNA), kcat= 0.00833/sec (RNA)
S148A
Km=0.0873 (UTP), kcat=0.021/sec (UTP), Km=0.0002 (RNA), kcat= 0.0166/sec (RNA)
S188A
Km=0.034 (UTP), kcat=0.0005/sec (UTP), Km=0.0003 (RNA), kcat= 0.00166/sec (RNA)
V271R/C83F
-
240% of wild-type activity for transfer to terminal U residue
additional information
-
mutations of metal coordinating catalytic aspartic residues D66, D68 and D136, render TUT4 inactive but have no effect on UTP binding
R327A
the activity of the mutant is reduced compared to the wild type enzyme. The mutant shows clear abrogation of the 3'-G specificity, whereby the 3'-G substrate is uridylated less readily than the 3'-U, 3'-A and 3'-C substrates
R327A
the uridylation efficiency of the mutant is reduced dramatically to about 4% when compared with that of wild type enzyme
R327K
the activity of the mutant is reduced compared to the wild type enzyme but the mutant shows selectivity for 3'-G and 3'-U RNA substrates, similar to the wild type enzyme
R327K
the uridylation efficiency of the mutant is reduced dramatically to about 4% when compared with that of wild type enzyme
R141A
Km=0.001 (UTP), kcat=0.00011/sec (UTP),Km=0.0726 (RNA), kcat= 0.0216/sec (RNA)
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression and purification of 20S editosome-associated RET2 complex from Trypanosoma brucei by affinity isolation
-
homogenous RET1 is purified from an enriched mitochondrial fraction of Leishmania tarentolae by a series of chromatographic steps: affinity chromatography (polyU Sepharose 4B), anion-exchange chromatography (Poros 20 HQ 46/100 column), gel filtration (Superose 12 and Superose 6 columns) and hydrophobic interactions chromatography (Phenyl Superose column)
-
Ni-NTA agarose column chromatography, HiTrap heparin column chromatography and Superdex 200 gel filtration
Ni-NTA column chromatography, HiTrap heparin column chromatography and Superdex 200 gel filtration
Ni-NTA resin column chromatography and Superdex 200 gel filtration
partial purification of U6 snRNA specific enzyme form via chromatography on a U6 snRNA affinity resin, separation from unspecific enzyme form
-
recombinant His-tagged wild-type and mutant TUT4 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ion exchange chromatography, and gel filtration
recombinant RET1 from Leishmania tarentolae is purified by cation-exchange resin (Sepharose S Fast Flow), metal affinity chromatography (Talon metal affinity column), anion-exchange chromatography (Mono Q 5/5 column), expected yield: 0.2-0.5 mg/liter
-
recombinant RET1 from Trypanosoma brucei is purified by metal affinity chromatography (Talon metal affinity column), anion-exchange chromatography (HiTrap Q column) and loading onto a MonoS 5/5 column (final purification step), expected yield is 0.5 mg/liter of bacterial culture, it is important to maintain the concentration of KCl above 80 mM during purification, as protein tends to precipitate under low salt conditions
-
the recombinant expressed RET2 is purified by loading the protein extract onto a Talon affinity column and onto a HiTrap Sepharose S column, the expected protein yield is 1 mg of protein per liter of bacterial culture
-
Ni-NTA agarose column chromatography, HiTrap heparin column chromatography and Superdex 200 gel filtration
Ni-NTA agarose column chromatography, HiTrap heparin column chromatography and Superdex 200 gel filtration
Ni-NTA resin column chromatography and Superdex 200 gel filtration
-
Ni-NTA resin column chromatography and Superdex 200 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA sequence determination, editosomal enzyme, expression as His-tagged protein in Escherichia coli
-
DNA sequence determination, gene is located on chromosome 9, expression as His-tagged protein in Escherichia coli
-
DNA sequence determination, mitochondrial enzyme, expression as His-tagged protein in Escherichia coli
-
expressed in Escherichia coli BL-21 as a 6xHis tagged fusion protein
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli Gold (DE3) cells
expression in Escherichia coli BL21(DE3) Codon Plus RIL, use of strains bearing additional tRNAs for expression of genes with G-rich codons is essential for RET1 expression
expression of RET2 in Leishmania tarentolae cells as cytosolic enzyme by removing the mitochondrial targeting signal sequence
-
for recombinant expression in Escherichia coli BL21 the RET2 gene lacking 21 codons at the 5' end, which correspond to the mitochondria importation signal, is cloned into pET15+vector to generate N-terminal 6 His-RET2 fusion protein
-
phylogenetic analysis, sequence comparison and signature motifs, overview
TbRET2 fused with the affinity TAP tag at the C-terminus using pLew79 vector in 29-13 cell line
-
TUT4, DNA and amino acid sequence determination and analysis, expression of N-terminally His-tagged wild-type and mutant TUT4 in Escherichia coli strain BL21(DE3)
expression in Escherichia coli BL21(DE3) Codon Plus RIL, use of strains bearing additional tRNAs for expression of genes with G-rich codons is essential for RET1 expression
-
expression in Escherichia coli BL21(DE3) Codon Plus RIL, use of strains bearing additional tRNAs for expression of genes with G-rich codons is essential for RET1 expression
-
phylogenetic analysis, sequence comparison and signature motifs, overview
-
phylogenetic analysis, sequence comparison and signature motifs, overview
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
a single C2H2-type zinc finger domain of Zcchc11 is responsible for the functional interaction with pluripotency factor Lin28. Lin28 uses terminal uridylyltransferases Zcchc11 and Zcchc6 to control let-7 expression and has important implications for stem cell biology as well as cancer
medicine
pluripotency factor Lin28 uses terminal uridylyltransferases Zcchc11 and Zcchc6 to control let-7 expression and has important implications for stem cell biology as well as cancer
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bakalara, N.; Simpson, A.M.; Simpson, L.
The Leishmania kinetoplast-mitochondrion contains terminal uridylyltransferase and RNA ligase activities
J. Biol. Chem.
264
18679-18686
1989
Leishmania tarentolae, Leishmania tarentolae UC
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Zabel, P.; Dorssers, L.; Wernars, K.; van Kammen, A.
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Homo sapiens
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Leishmania tarentolae, Trypanosoma brucei
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Homo sapiens
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Trypanosoma brucei
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T. brucei RNA editing: action of the U-insertional TUTase within a U-deletion cycle
RNA
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Trypanosoma brucei, Trypanosoma brucei TREU-667
brenda
Aphasizhev, R.; Aphasizheva, I.
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Leishmania tarentolae, Trypanosoma brucei
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Mono-uridylation of pre-microRNA as a key step in the biogenesis of group II let-7 microRNAs
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Homo sapiens (Q5TAX3), Homo sapiens (Q5VYS8)
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Stagno, J.; Aphasizheva, I.; Bruystens, J.; Luecke, H.; Aphasizhev, R.
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Mechanism of U insertion RNA editing in trypanosome mitochondria: the bimodal TUTase activity of the core complex
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Trypanosoma brucei
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Strand-asymmetric endogenous Tetrahymena small RNA production requires a previously uncharacterized uridylyltransferase protein partner
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Tetrahymena thermophila (I1Y9V9)
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Thornton, J.E.; Chang, H.M.; Piskounova, E.; Gregory, R.I.
Lin28-mediated control of let-7 microRNA expression by alternative TUTases Zcchc11 (TUT4) and Zcchc6 (TUT7)
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Homo sapiens (Q5TAX3), Homo sapiens (Q5VYS8)
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Uridylation of RNA hairpins by tailor confines the emergence of microRNAs in Drosophila
Mol. Cell
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Drosophila melanogaster (Q9VI58)
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Sement, F.M.; Ferrier, E.; Zuber, H.; Merret, R.; Alioua, M.; Deragon, J.M.; Bousquet-Antonelli, C.; Lange, H.; Gagliardi, D.
Uridylation prevents 3 trimming of oligoadenylated mRNAs
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Arabidopsis thaliana (O64642), Arabidopsis thaliana Col-0 (O64642)
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Distinct and cooperative activities of HESO1 and URT1 nucleotidyl transferases in microRNA turnover in Arabidopsis
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Arabidopsis thaliana (O64642), Arabidopsis thaliana (Q5XET5)
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Nucleotide specificity of the human terminal nucleotidyltransferase Gld2 (TUT2)
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Homo sapiens
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Zhu, L.; Hu, Q.; Cheng, L.; Jiang, Y.; Lv, M.; Liu, Y.; Li, F.; Shi, Y.; Gong, Q.
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Arabidopsis thaliana (O64642)
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Function and regulation of human terminal uridylyltransferases
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Homo sapiens (F5H0R1), Homo sapiens (Q5TAX3), Homo sapiens (Q5VYS8)
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Evolution of miRNA tailing by 3' terminal uridylyl transferases in Metazoa
Genome Biol. Evol.
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Amphimedon queenslandica, Drosophila melanogaster, Hydra vulgaris, Nematostella vectensis
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George, J.T.; Azhar, M.; Aich, M.; Sinha, D.; Ambi, U.B.; Maiti, S.; Chakraborty, D.; Srivatsan, S.G.
Terminal uridylyl transferase mediated site-directed access to clickable chromatin employing CRISPR-dCas9
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Schizosaccharomyces pombe
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Kim, H.; Kim, J.; Yu, S.; Lee, Y.Y.; Park, J.; Choi, R.J.; Yoon, S.J.; Kang, S.G.; Kim, V.N.
A mechanism for microRNA arm switching regulated by uridylation
Mol. Cell
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Homo sapiens (Q5TAX3), Homo sapiens (Q5VYS8)
brenda
Yamashita, S.; Nagaike, T.; Tomita, K.
Crystal structure of the Lin28-interacting module of human terminal uridylyltransferase that regulates let-7 expression
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Homo sapiens (Q5TAX3), Homo sapiens
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Yamashita, S.; Takagi, Y.; Nagaike, T.; Tomita, K.
Crystal structures of U6 snRNA-specific terminal uridylyltransferase
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15788
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Homo sapiens (F5H0R1), Homo sapiens
brenda
Kroupova, A.; Ivascu, A.; Reimao-Pinto, M.M.; Ameres, S.L.; Jinek, M.
Structural basis for acceptor RNA substrate selectivity of the 3 terminal uridylyl transferase Tailor
Nucleic Acids Res.
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Drosophila melanogaster (Q9VI58)
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Chung, C.; Jaramillo, J.; Ellis, M.; Bour, D.; Seidl, L.; Jo, D.; Turk, M.; Mann, M.; Bi, Y.; Haniford, D.; Duennwald, M.; Heinemann, I.
RNA surveillance by uridylation-dependent RNA decay in Schizosaccharomyces pombe
Nucleic Acids Res.
47
3045-3057
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Schizosaccharomyces pombe, Schizosaccharomyces pombe BG 0000H6
brenda
Cheng, L.; Li, F.; Jiang, Y.; Yu, H.; Xie, C.; Shi, Y.; Gong, Q.
Structural insights into a unique preference for 3 terminal guanine of mirtron in Drosophila TUTase Tailor
Nucleic Acids Res.
47
495-508
2019
Drosophila melanogaster (Q9VI58)
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Xu, K.; Lin, J.; Zandi, R.; Roth, J.A.; Ji, L.
MicroRNA-mediated target mRNA cleavage and 3-uridylation in human cells
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30242
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Homo sapiens
brenda
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