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sulfide + adenylated-tRNA-uridine(position8)
tRNA-4-thiouridine(position8) + ?
-
sulfide is able to replace IscS/cysteine as a substrate for 4-thiouridine synthesis
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
additional information
?
-
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
-
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
-
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
-
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
-
-
-
ir
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
the biosynthesis of 4-thiouridine in Escherichia coli tRNA requires the action of both the thiamine pathway enzyme ThiI and the cysteine desulfurase IscS. IscS catalyzes sulfur transfer from L-cysteine to ThiI, which utilizes MgATP2- to activate uridine 8 in tRNA and transfers sulfur to give s4U
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
ThiI is a recipient of S(0) from IscS and catalyzes the ultimate sulfur transfer step in the biosynthesis of 4-thiouridine
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
Cys456 bears a persulfide group upon incubation with sulfurtransferase IscS and cysteine, no intermediate sulfur carrier protein is chemically required
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
sulfane sulfur generated by IscS is transferred sequentially to ThiI and then to tRNA during the in vitro synthesis of 4-thiouridine
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
the biosynthesis of 4-thiouridine in Escherichia coli tRNA requires the action of both the thiamin pathway enzyme ThiI and the cysteine desulfurase IscS. IscS catalyzes sulfur transfer from L-cysteine to ThiI, which utilizes MgATP2- to activate uridine 8 in tRNA and transfers sulfur to give s4U. Outside of the modified uridine 8, there is no primary sequence requirement for substrate recognition. However, the secondary and tertiary structure restrictions appear sufficient to explain why s4U modification is limited in the cell to tRNA
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
ThiI receives the sulfur transferred from the persulfide group of the sulfurtransferase IscS. Formation of a disulfide bond between Cys-344 and Cys-456 of ThiI. Evidence for the persulfideĀdisulfideĀthiol cycle at Cys-456 of ThiI
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
two mechanisms for the sulfur transfer mediated by ThiI are proposed: A. mechanism providing for the direct nucleophilic attack on an activated uridine species by the terminal sulfur of the persulfide on Cys-456 of ThiI. B. mechanism in which ThiI functions to generate hydrogen sulfide, which subsequently serves as the nucleophile to displace the activated oxygen of uridine 8
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
-
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
-
-
?
additional information
?
-
-
ThiI is responsible for the formation of the modified base 4-thiouridine found at position 8 in some prokaryotic tRNAs. This base acts as a sensitive trigger for the response mechanism to UV exposure, providing protection against its damaging effects
-
-
?
additional information
?
-
-
the enzyme is not able to enhance cysteine desulfurase NifZ activity of sulfide or alanine formation
-
-
?
additional information
?
-
-
the enzyme is not able to enhance cysteine desulfurase NifZ activity of sulfide or alanine formation
-
-
?
additional information
?
-
-
the enzyme also catalyzes the transfer of sulfur from thiosulfate to cyanide (EC 2.8.1.1)
-
-
?
additional information
?
-
-
the RLD-containing protein ThiI also acts as a sulfur carrier for generating ThiS-COSH. ThiI accepts a persulfide sulfur from IscS, then transfers the sulfur for thiocarboxylate formation to the C-terminus of ThiS which is catalyzed by ThiF
-
-
?
additional information
?
-
-
three domains of ThiI are essential for the thiolation of tRNA: a THUMP domain that binds tRNA, an AANH domain that activates the uridine residue by adenylylation, and a rhodanese domain that transfers sulfur to the activated uridine residue. Only the rhodanese domain of the ThiI protein is required for a key thiolation reaction in the synthesis of thiamine, while the other two domains (THUMP and AANH) are dispensable
-
-
?
additional information
?
-
-
the enzyme also displays an ATP diphosphatase activity for the adenylation of uridine
-
-
?
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sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
additional information
?
-
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
-
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
-
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
-
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
-
-
-
ir
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
the biosynthesis of 4-thiouridine in Escherichia coli tRNA requires the action of both the thiamine pathway enzyme ThiI and the cysteine desulfurase IscS. IscS catalyzes sulfur transfer from L-cysteine to ThiI, which utilizes MgATP2- to activate uridine 8 in tRNA and transfers sulfur to give s4U
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
ThiI is a recipient of S(0) from IscS and catalyzes the ultimate sulfur transfer step in the biosynthesis of 4-thiouridine
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
-
-
-
?
sulfurtransferase IscS-SSH + adenylated-tRNA-uridine(position8)
sulfurtransferase IscS-SH + tRNA-4-thiouridine(position8) + AMP
-
-
-
?
additional information
?
-
-
ThiI is responsible for the formation of the modified base 4-thiouridine found at position 8 in some prokaryotic tRNAs. This base acts as a sensitive trigger for the response mechanism to UV exposure, providing protection against its damaging effects
-
-
?
additional information
?
-
-
the enzyme is not able to enhance cysteine desulfurase NifZ activity of sulfide or alanine formation
-
-
?
additional information
?
-
-
the enzyme is not able to enhance cysteine desulfurase NifZ activity of sulfide or alanine formation
-
-
?
additional information
?
-
-
three domains of ThiI are essential for the thiolation of tRNA: a THUMP domain that binds tRNA, an AANH domain that activates the uridine residue by adenylylation, and a rhodanese domain that transfers sulfur to the activated uridine residue. Only the rhodanese domain of the ThiI protein is required for a key thiolation reaction in the synthesis of thiamine, while the other two domains (THUMP and AANH) are dispensable
-
-
?
additional information
?
-
-
the enzyme also displays an ATP diphosphatase activity for the adenylation of uridine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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malfunction
-
Bacillus subtilis strains lacking thiI display a specific disruption in the C-4 thiolation of the uridine base at position 8 of tRNA synthesis
malfunction
-
deletion of ThiI (MMP1354) abolishes the biosynthesis of 4-thiouridine but not of thiamine
malfunction
-
thiI mutants are auxotrophic for thiamine, specifically for the thiazole component of this essential vitamin
malfunction
-
Bacillus subtilis strains lacking thiI display a specific disruption in the C-4 thiolation of the uridine base at position 8 of tRNA synthesis
-
metabolism
-
the enzyme is crucial for the formation of C-4 thiolation of the uridine base at position 8 of tRNA modification in tRNA
metabolism
-
ThiI is a bifunctional enzyme required for the synthesis of both the 4-thiouridine modification in tRNA and the thiazole moiety of thiamine. In 4-thiouridine biosynthesis, ThiI adenylates the tRNA uridine and transfers sulfur from a persulfide formed on the protein. The C-terminal rhodanese domain of ThiI is sufficient for thiazole synthesis in vivo
metabolism
-
the enzyme is crucial for the formation of C-4 thiolation of the uridine base at position 8 of tRNA modification in tRNA
-
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crystal structure of Bacillus anthracis ThiI in complex with AMP
-
in complex with a truncated tRNA, sitting drop vapor diffusion method, using 2 M sodium formate, 100 mM sodium citrate, pH 4.6, 2 mM dithiothreitol
in complex with RNA (truncated tRNAPhe), sitting drop vapor diffusion method, using 2 M sodium formate, 100 mM sodium citrate pH 4.6, 2 mM dithiothreitol, at 20Ā°C
sitting drop vapor diffusion method, using 2.0 M sodium formate, 100 mM sodium citrate pH 4.6, 2 mM dithiothreitol
THiI-tRNA complex and selenium-ThiI-tRNA complex, 3.1 A resolution
-
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Wright, C.M.; Palenchar, P.M.
Mueller, E.G.: A paradigm for biological sulfur transfers via persulfide groups: a persulfide-disulfide-thiol cycle in 4-thiouridine biosynthesis.
Chem. Commun. (Camb. )
2002
2708-2709
2002
Escherichia coli
brenda
Wright, C.M.; Christman, G.D.; Snellinger, A.M.; Johnston, M.V.; Mueller, E.G.
Direct evidence for enzyme persulfide and disulfide intermediates during 4-thiouridine biosynthesis
Chem. Commun. (Camb. )
2006
3104-3106
2006
Escherichia coli
brenda
Kambampati, R.; Lauhon, C.T.
Evidence for the transfer of sulfane sulfur from IscS to ThiI during the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA
J. Biol. Chem.
275
10727-10730
2000
Escherichia coli
brenda
Mueller, E.; Palenchar, P.; Buck, C.
The role of the cysteine residues of ThiI in the generation of 4-thiouridine in tRNA
J. Biol. Chem.
276
33588-33595
2001
Escherichia coli
brenda
Lauhon, C.; Erwin, W.; Ton, G.
Substrate specificity for 4-thiouridine modification in Escherichia coli
J. Biol. Chem.
279
23022-23029
2004
Escherichia coli
brenda
Waterman, D.; Ortiz-Lombardia, M.; Fogg, M.; Koonin, E.; Antson, A.
Crystal structure of Bacillus anthracis ThiI, a tRNA-modifying enzyme containing the predicted RNA-binding THUMP domain
J. Mol. Biol.
356
97-110
2006
Bacillus anthracis
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
brenda
Naumann, P.-T.
Versuche zur Strukturaufklärung bakterieller Thiouridin Synthetasen
PH. D. Thesis Universität Göttingen
2005
0000
2005
Escherichia coli, Thermotoga maritima
-
brenda
Naumann, P.T.; Lauhon, C.T.; Ficner, R.
Purification, crystallization and preliminary crystallographic analysis of a 4-thiouridine synthetase-RNA complex
Acta Crystallogr. Sect. F
69
421-424
2013
Thermotoga maritima (Q9X220), Thermotoga maritima
brenda
Bender, R.
The danger of annotation by analogy: Most thiI genes play no role in thiamine biosynthesis
J. Bacteriol.
193
4574-4575
2011
Escherichia coli
brenda
Martinez-Gomez, N.C.; Palmer, L.D.; Vivas, E.; Roach, P.L.; Downs, D.M.
The rhodanese domain of ThiI is both necessary and sufficient for synthesis of the thiazole moiety of thiamine in Salmonella enterica
J. Bacteriol.
193
4582-4587
2011
Salmonella enterica
brenda
Rajakovich, L.J.; Tomlinson, J.; Dos Santos, P.C.
Functional analysis of Bacillus subtilis genes involved in the biosynthesis of 4-thiouridine in tRNA
J. Bacteriol.
194
4933-4940
2012
Bacillus subtilis, Bacillus subtilis PS832
brenda
Boschi-Muller, S.; Motorin, Y.
Chemistry enters nucleic acids biology: enzymatic mechanisms of RNA modification
Biochemistry
78
1392-1404
2013
Escherichia coli
brenda
Neumann, P.; Lakomek, K.; Naumann, P.T.; Erwin, W.M.; Lauhon, C.T.; Ficner, R.
Crystal structure of a 4-thiouridine synthetase-RNA complex reveals specificity of tRNA U8 modification
Nucleic Acids Res.
42
6673-6685
2014
Thermotoga maritima (Q9X220), Thermotoga maritima, Thermotoga maritima ATCC 43589 (Q9X220)
brenda
Veerareddygari, G.R.; Klusman, T.C.; Mueller, E.G.
Characterization of the catalytic disulfide bond in E. coli 4-thiouridine synthetase to elucidate its functional quaternary structure
Protein Sci.
25
1737-1743
2016
Escherichia coli
brenda