4.5 Article

Selenomodification of tRNA in archaea requires a bipartite rhodanese enzyme

期刊

FEBS LETTERS
卷 586, 期 6, 页码 717-721

出版社

WILEY
DOI: 10.1016/j.febslet.2012.01.024

关键词

Selenouridine; tRNA 2-selenouridine synthase; YbbB; Archaea; Methanococcus maripaludis

资金

  1. Division of Chemical Sciences, Geosciences, and Biosciences, Office of Basic Energy Sciences of the U.S. Department of Energy [DE-FG02-98ER20311]
  2. National Institute of General Medical Sciences [GM22854]
  3. COMBREX, via the National Institute of General Medical Sciences [1RC2GM092602-01]

向作者/读者索取更多资源

5-Methylaminomethyl-2-selenouridine (mnm(5)Se(2)U) is found in the first position of the anticodon in certain tRNAs from bacteria, archaea and eukaryotes. This selenonucleoside is formed in Escherichia coli from the corresponding thionucleoside mnm(5)S(2)U by the monomeric enzyme YbbB. This nucleoside is present in the tRNA of Methanococcales, yet the corresponding 2-selenouridine synthase is unknown in archaea and eukaryotes. Here we report that a bipartite ybbB ortholog is present in all members of the Methanococcales. Gene deletions in Methanococcus maripaludis and in vitro activity assays confirm that the two proteins act in trans to form in tRNA a selenonucleoside, presumably mnm(5)Se(2)U. Phylogenetic data suggest a primal origin of seleno-modified tRNAs. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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