New light on methylthiolation reactions.
A novel enzyme, named RimO for ribosomal modification (Anton et al., 2008) catalyzes the methylthiolation of aspartate 88 of the S12 ribosomal protein in Escherichia coli and shows a strong similarity with the iron-sulfur enzyme MiaB involved in the methylthiolation of tRNAs.
Fontecave
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Laboratoire de Chimie et Biologie des Métaux, UMR 5249, Université Joseph Fourier, CEA, CNRS, 17 Avenue des Martyrs, 38054 Grenoble Cedex 9, France. M.Fontecave.mfontecave@cea.fr
Mulliez
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Atta
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D001224:Aspartic Acid / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000378:metabolism; D008697:Methane / Q000031:analogs & derivatives / Q000378:metabolism*; D012343:RNA, Transfer / Q000378:metabolism; D012269:Ribosomal Proteins / Q000737:chemistry / Q000378:metabolism; D013438:Sulfhydryl Compounds / Q000737:chemistry / Q000378:metabolism*; D013466:Sulfurtransferases / Q000378:metabolism
D029968:Escherichia coli Proteins; D012269:Ribosomal Proteins; D013438:Sulfhydryl Compounds; C034212:ribosomal protein S12; D001224:Aspartic Acid; D012343:RNA, Transfer; C499584:MiaB protein, E coli; D013466:Sulfurtransferases; D008697:Methane