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J. Biol. Chem., Vol. 279, Issue 46, 47555-47563, November 12, 2004

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MiaB Protein Is a Bifunctional Radical-S-Adenosylmethionine Enzyme Involved in Thiolation and Methylation of tRNA^*

Fabien Pierrel, Thierry Douki, Marc Fontecave¶, and Mohamed Atta||

From the Laboratoire de Chimie et Biochimie des Centres Rédox Biologiques, DRDC-CB, Unité Mixte de Recherche 5047 Commissariat à l'Energie Atomique/CNRS/Université Joseph Fourier and the Laboratoire Lesions des Acides Nucleiques, Service de Chimie Inorganique et Biologique, CEA/DSM/Département de Recherche Fondamentale sur la Matière Condensée, CEA-Grenoble, 17 Avenue des Martyrs, 38054 Grenoble Cedex 09, France

The last biosynthetic step for 2-methylthio-N⁶-isopentenyl-adenosine (ms²i⁶A), present at position 37 in some tRNAs, consists of 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 (AdoMet), and a reducing agent. We show that a synthetic i⁶A-containing RNA corresponding to the anticodon stem loop of tRNA^Phe 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 AdoMet is converted to 5'-deoxyadenosine, probably through reductive cleavage and intermediate formation ofa5'-deoxyadenosyl radical as observed in other "Radical-AdoMet" enzymes, and a second molecule of AdoMet is used as a methyl donor as shown by labeling experiments. The origin of the sulfur atom is discussed.

Received for publication, July 28, 2004 , and in revised form, August 30, 2004.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence may be addressed: DRDC-CB, CEA-Grenoble, 38054 Grenoble, France. Fax: 0033438789124; E-mail: mfontecave{at}cea.fr. || To whom correspondence may be addressed: DRDC-CB, CEA-Grenoble, 38054 Grenoble, France. Fax: 0033438789124; E-mail: mohamed.atta{at}cea.fr.

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