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The putative tRNA 2-thiouridine synthetase Ncs6 is an essential sulfur carrier in Methanococcus maripaludis.

FEBS Lett.2014 Mar 18;588(6):873-7. Epub 2014 Feb 11
Yuchen Liu 1 , Feng Long 2 , Liangliang Wang 2 , Dieter Söll 3 , William B Whitman 2
Yuchen Liu 1 , Feng Long 2 , Liangliang Wang 2 , Dieter Söll 3 , William B Whitman 2

[No authors listed]

Author information
  • 1 Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA. Electronic address: yuchen.l@yale.edu.
  • 2 Department of Microbiology, University of Georgia, Athens, GA 30602-2605, USA.
  • 3 Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8114, USA; Department of Chemistry, Yale University, New Haven, CT 06520-8114, USA.

摘要

Thiolation of carbon-2 of uridine located in the first position of the anticodons of tRNAUUG(Gln), tRNAUUC(Glu), and tRNAUUU(Lys) is a conserved RNA modification event requiring the 2-thiouridine synthetase Ncs6/Ctu1 in archaea and eukaryotes. Ncs6/Ctu1 activates uridine by adenylation, but its role in sulfur transfer is unclear. Here we show that Mmp1356, the Ncs6/Ctu1 homolog in the archaeon Methanococcus maripaludis, forms a persulfide enzyme adduct with an active site cysteine; this suggests that Mmp1356 directly participates in sulfur transfer as a persulfide carrier. Transposon mutagenesis shows that Mmp1356 is likely to be an essential protein.

KEYWORDS: 2-Thiouridine, Archaea, Methanogen, Sulfur, tRNA modification

基因

MMP_RS06995

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