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Papers In Press, published online ahead of print September 2, 2004
DRDC/CB, CEA/GRENOBLE, Grenoble, Grenoble 38054
Corresponding Author: mohamed.atta{at}cea.fr
The last biosynthetic step for 2-methylthio-N-6-isopentenyl-adenosine (ms2i6A), present at position 37 in some tRNAs, consists in the methylthiolation of the isopentenyl-adenosine (i6A) precursor. In this work we have reconstituted in vitro the conversion of i6A to ms2i6A within a tRNA substrate using the iron-sulfur MiaB protein, S-adenosylmethionine (SAM) and a reducing agent. We show that a synthetic i6A-containing RNA corresponding to the anticodon stem loop of tRNAPhe is also a substrate. This study demonstrates that MiaB protein is a bifunctional system, involved in both thiolation and methylation of i6A. In this process, one molecule of SAM is converted to 5’-deoxyadenosine, probably through reductive cleavage and intermediate formation of a 5’-deo xyadenosyl radical as observed in other “Radical-SAM” enzymes, and a second molecule of SAM is used as a methyl donor as shown by labelling experiments. The origin of the sulfur atom is discussed$t
J. Biol. Chem, 10.1074/jbc.M408562200
Submitted on July 28, 2004
Revised on August 30, 2004
Accepted on August 30, 2004
MiaB protein is a bifunctional
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