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Selenomodification of tRNA in archaea requires a bipartite rhodanese enzyme
Author(s) -
Su Dan,
Ojo Temitope T.,
Söll Dieter,
Hohn Michael J.
Publication year - 2012
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.2012.01.024
Subject(s) - methanococcus , transfer rna , archaea , biology , escherichia coli , biochemistry , genetics , gene , enzyme , rna
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.