Selenomodification of tRNA in archaea requires a bipartite rhodanese enzyme

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Abstract

5-Methylaminomethyl-2-selenouridine (mnm 5Se 2U) 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 5S 2U 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 5Se 2U. Phylogenetic data suggest a primal origin of seleno-modified tRNAs. © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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Su, D., Ojo, T. T., Söll, D., & Hohn, M. J. (2012). Selenomodification of tRNA in archaea requires a bipartite rhodanese enzyme. FEBS Letters, 586(6), 717–721. https://doi.org/10.1016/j.febslet.2012.01.024

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