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a [protein]-S-sulfanyl-L-cysteine + uridine34 in tRNA + ATP + reduced acceptor
a [protein]-L-cysteine + 2-thiouridine34 in tRNA + AMP + diphosphate + acceptor
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
additional information
?
-
a [protein]-S-sulfanyl-L-cysteine + uridine34 in tRNA + ATP + reduced acceptor
a [protein]-L-cysteine + 2-thiouridine34 in tRNA + AMP + diphosphate + acceptor
-
enzyme adenylates and subsequently thiolates tRNA to form the s2U modification
-
?
a [protein]-S-sulfanyl-L-cysteine + uridine34 in tRNA + ATP + reduced acceptor
a [protein]-L-cysteine + 2-thiouridine34 in tRNA + AMP + diphosphate + acceptor
-
enzyme adenylates and subsequently thiolates tRNA to form the s2U modification
-
?
a [protein]-S-sulfanyl-L-cysteine + uridine34 in tRNA + ATP + reduced acceptor
a [protein]-L-cysteine + 2-thiouridine34 in tRNA + AMP + diphosphate + acceptor
-
the enzyme functions on tRNALys(mnm5s2UUU), tRNAGlu(mnm5s2UUC), and tRNAGln((c)mnm5s2UUG)
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-
?
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
-
-
-
?
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
MnmA catalyzes a sulfuration reaction to synthesize 2-thiouridine at the wobble positions of tRNAGlu, tRNAGln and tRNALys in Escherichia coli
-
-
?
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
the biogenesis of 2-thiouridine in Escherichia coli utilizes persulfide chemistry and proceeds through a complex sulfur-relay system by multiple sulfur mediators that select and facilitate specific sulfur flow to 2-thiouridine from various cellular sulfur pathways. TusE interacts with MnmA, a thiouridylase responsible for 2-thiouridine formation, and transfers the persulfide to it. MnmA activates the C2-position of the uracil base at the wobble position of the tRNA by forming an acyl-adenylated intermediate. Then, nucleophilic attack by the persulfide sulfur on the activated carbon generates a thiocarbonyl group by releasing the AMP
-
-
?
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
the wobble bases of bacterial tRNAs responsible for NNR codons are modified to 5-methylaminomethyl-2-thiouridine (mnm5s2U). 2-thio modification of mnm5s2U is required for accurate decoding and essential for normal cell growth. IscS and MnmA are the minimum essential factors for 2-thiolation of mnm5s2U in vitro. TusE directly interacts with MnmA-tRNA to form a ternary complex. TusE appears to interact with MnmA, but not with tRNA, because TusE-tRNA interactions are not observed
-
-
?
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
TusE interacts with MnmA, a thiouridylase responsible for 2-thiouridine formation, and transfers the persulfide to it. MnmA activates the C2-position of the uracil base at the wobble position of the tRNA by forming an acyl-adenylated intermediate. Then, nucleophilic attack by the persulfide sulfur on the activated carbon generates a thiocarbonyl group by releasing the AMP
-
-
?
additional information
?
-
thionucleosides are uniquely present in tRNA. In many organisms, tRNAs specific for Lys, Glu, and Gln contain hypermodified 2-thiouridine (s2U) derivatives at wobble position 34. The s2 group of s2U34 stabilizes anticodon structure, confers ribosome binding ability to tRNA and improves reading frame maintenance
-
-
?
additional information
?
-
thionucleosides are uniquely present in tRNA. In many organisms, tRNAs specific for Lys, Glu, and Gln contain hypermodified 2-thiouridine (s2U) derivatives at wobble position 34. Purified IscS-persulfide is able to provide sulfur for in vitro s2U synthesis in the absence of cysteine. The s2 group of s2U34 stabilizes anticodon structure, confers ribosome binding ability to tRNA and improves reading frame maintenance. Identification of 2-thiouridine as product of the in vitro s2U reaction.
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?
additional information
?
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-
in the IscSeMnmA pathway, protein MnmA, together with the cysteine desulfurase IscS and sulfur transfer mediators TusA-E, performs thiolation at position 2 of U34, which occurs only in tRNALys mnm5s2UUU, tRNAGlu mnm5s2UUC, tRNAGln cmnm5s2UUG
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-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
a [protein]-S-sulfanyl-L-cysteine + uridine34 in tRNA + ATP + reduced acceptor
a [protein]-L-cysteine + 2-thiouridine34 in tRNA + AMP + diphosphate + acceptor
-
the enzyme functions on tRNALys(mnm5s2UUU), tRNAGlu(mnm5s2UUC), and tRNAGln((c)mnm5s2UUG)
-
-
?
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
additional information
?
-
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
MnmA catalyzes a sulfuration reaction to synthesize 2-thiouridine at the wobble positions of tRNAGlu, tRNAGln and tRNALys in Escherichia coli
-
-
?
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
the biogenesis of 2-thiouridine in Escherichia coli utilizes persulfide chemistry and proceeds through a complex sulfur-relay system by multiple sulfur mediators that select and facilitate specific sulfur flow to 2-thiouridine from various cellular sulfur pathways. TusE interacts with MnmA, a thiouridylase responsible for 2-thiouridine formation, and transfers the persulfide to it. MnmA activates the C2-position of the uracil base at the wobble position of the tRNA by forming an acyl-adenylated intermediate. Then, nucleophilic attack by the persulfide sulfur on the activated carbon generates a thiocarbonyl group by releasing the AMP
-
-
?
TusE-SSH + adenylated-tRNA-uridine
TusE-SH + tRNA-2-thiouridine + AMP
the wobble bases of bacterial tRNAs responsible for NNR codons are modified to 5-methylaminomethyl-2-thiouridine (mnm5s2U). 2-thio modification of mnm5s2U is required for accurate decoding and essential for normal cell growth. IscS and MnmA are the minimum essential factors for 2-thiolation of mnm5s2U in vitro. TusE directly interacts with MnmA-tRNA to form a ternary complex. TusE appears to interact with MnmA, but not with tRNA, because TusE-tRNA interactions are not observed
-
-
?
additional information
?
-
thionucleosides are uniquely present in tRNA. In many organisms, tRNAs specific for Lys, Glu, and Gln contain hypermodified 2-thiouridine (s2U) derivatives at wobble position 34. The s2 group of s2U34 stabilizes anticodon structure, confers ribosome binding ability to tRNA and improves reading frame maintenance
-
-
?
additional information
?
-
-
in the IscSeMnmA pathway, protein MnmA, together with the cysteine desulfurase IscS and sulfur transfer mediators TusA-E, performs thiolation at position 2 of U34, which occurs only in tRNALys mnm5s2UUU, tRNAGlu mnm5s2UUC, tRNAGln cmnm5s2UUG
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Kambampati, R.; Lauhon, C.T.
MnmA and IscS are required for in vitro 2-thiouridine biosynthesis in Escherichia coli
Biochemistry
42
1109-1117
2003
Escherichia coli (P25745)
brenda
Numata, T.; Ikeuchi, Y.; Fukai, S.; Suzuki, T.; Nureki, O.
Snapshots of tRNA sulphuration via an adenylated intermediate
Nature
442
419-424
2006
Escherichia coli (P25745)
brenda
Numata, T.; Ikeuchi, Y.; Fukai, S.; Adachi, H.; Matsumura, H.; Takano, K.; Murakami, S.; Inoue, T.; Mori, Y.; Sasaki, T.; Suzuki, T.; Nureki, O.
Crystallization and preliminary X-ray analysis of the tRNA thiolation enzyme MnmA from Escherichia coli complexed with tRNA(Glu)
Acta Crystallogr. Sect. F
62
368-371
2006
Escherichia coli (P25745)
brenda
Ikeuchi, Y.; Shigi, N.; Kato, J.; Nishimura, A.; Suzuki, T.
Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions.
Mol. Cell
21
97-108
2006
Escherichia coli (P25745)
brenda
Noma, A.; Sakaguchi, Y.; Suzuki, T.
Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridine biogenesis at tRNA wobble positions
Nucleic Acids Res.
37
1335-1352
2009
Escherichia coli (P25745)
brenda
Naumann, P.-T.
Versuche zur Strukturaufklärung bakterieller Thiouridin Synthetasen
PH. D. Thesis Universität Göttingen
2005
0000
2005
Thermotoga maritima, Escherichia coli (P25745)
-
brenda
Armengod, M.E.; Moukadiri, I.; Prado, S.; Ruiz-Partida, R.; Benitez-Paez, A.; Villarroya, M.; Lomas, R.; Garzon, M.J.; Martinez-Zamora, A.; Meseguer, S.; Navarro-Gonzalez, C.
Enzymology of tRNA modification in the bacterial MnmEG pathway
Biochimie
94
1510-1520
2012
Escherichia coli
brenda
Black, K.A.; Dos Santos, P.C.
Abbreviated pathway for biosynthesis of 2-thiouridine in Bacillus subtilis
J. Bacteriol.
197
1952-1962
2015
Bacillus subtilis (O35020), Bacillus subtilis 168 (O35020)
brenda
Armengod, M.E.; Meseguer, S.; Villarroya, M.; Prado, S.; Moukadiri, I.; Ruiz-Partida, R.; Garzon, M.J.; Navarro-Gonzalez, C.; Martinez-Zamora, A.
Modification of the wobble uridine in bacterial and mitochondrial tRNAs reading NNA/NNG triplets of 2-codon boxes
RNA Biol.
11
1495-1507
2014
Escherichia coli
brenda