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The putative tRNA 2‐thiouridine synthetase Ncs6 is an essential sulfur carrier in Methanococcus maripaludis
Author(s) -
Liu Yuchen,
Long Feng,
Wang Liangliang,
Söll Dieter,
Whitman William B.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.01.065
Subject(s) - methanococcus , transfer rna , archaea , biochemistry , aminoacyl trna synthetase , mutagenesis , uridine , biology , chemistry , genetics , gene , rna , mutation
Thiolation of carbon‐2 of uridine located in the first position of the anticodons oftRNA UUG GlntRNA UUC GluandtRNA UUU Lysis 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.