New light on methylthiolation reactions

M Fontecave; E Mulliez; M Atta

doi:10.1016/j.chembiol.2008.02.011

New light on methylthiolation reactions

Chem Biol. 2008 Mar;15(3):209-10. doi: 10.1016/j.chembiol.2008.02.011.

Authors

M Fontecave¹, E Mulliez, M Atta

Affiliation

¹ 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

PMID: 18355719
DOI: 10.1016/j.chembiol.2008.02.011

Abstract

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.

MeSH terms

Aspartic Acid / metabolism
Escherichia coli / metabolism
Escherichia coli Proteins / metabolism
Methane / analogs & derivatives
Methane / metabolism*
RNA, Transfer / metabolism
Ribosomal Proteins / chemistry
Ribosomal Proteins / metabolism
Sulfhydryl Compounds / chemistry
Sulfhydryl Compounds / metabolism*
Sulfurtransferases / metabolism

Substances

Escherichia coli Proteins
Ribosomal Proteins
Sulfhydryl Compounds
ribosomal protein S12
Aspartic Acid
RNA, Transfer
MiaB protein, E coli
Sulfurtransferases
Methane