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

FEBS Lett. 2014 Mar 18;588(6):873-7. doi: 10.1016/j.febslet.2014.01.065. Epub 2014 Feb 11.

Abstract

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Amino Acyl-tRNA Synthetases / chemistry*
  • Amino Acyl-tRNA Synthetases / genetics
  • Amino Acyl-tRNA Synthetases / metabolism
  • Archaeal Proteins / chemistry*
  • Archaeal Proteins / genetics
  • Archaeal Proteins / metabolism
  • Catalytic Domain
  • Conserved Sequence
  • Genes, Archaeal
  • Genes, Essential
  • Methanococcus / enzymology*
  • Methanococcus / genetics
  • Protein Binding
  • Protein Interaction Mapping
  • RNA, Transfer / biosynthesis
  • Sulfur / chemistry*
  • Sulfur / metabolism

Substances

  • Archaeal Proteins
  • Sulfur
  • RNA, Transfer
  • Amino Acyl-tRNA Synthetases