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J. Biol. Chem., Vol. 279, Issue 40, 41398-41403, October 1, 2004

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Involvement of the Molybdenum Cofactor Biosynthetic Machinery in the Maturation of the Escherichia coli Nitrate Reductase A^*

Alexandra Vergnes, Kamila Gouffi-Belhabich¶, Francis Blasco, Gérard Giordano, and Axel Magalon||

From the Laboratoire de Chimie Bactérienne, Institut Biologie Structurale et Microbiologie, CNRS 31, chemin Joseph Aiguier cedex 09, 13402 Marseille, France

The maturation of Escherichia coli nitrate reductase A requires the incorporation of the Mo-(bis-MGD) cofactor to the apoprotein. For this process, the NarJ chaperone is strictly required (Blasco, F., Dos Santos, J. P., Magalon, A., Frixon, C., Guigliarelli, B., Santini, C. L., and Giordano, G. (1998) Mol. Microbiol. 28, 435–447). We report the first description of protein interactions between molybdenum cofactor biosynthetic proteins (MogA, MoeA, MobA, and MobB) and the aponitrate reductase (NarG) using a bacterial two-hybrid approach. Two conditions have to be satisfied to allow the visualization of the interactions, (i) the presence of an active and mature molybdenum cofactor and (ii) the presence of the NarJ chaperone and of the NarG structural partner subunit, NarH. Formation of tungsten-substituted cofactor prevents the interaction between NarG and the four biosynthetic proteins. Our results suggested that the final stages of molybdenum cofactor biosynthesis occur on a complex made up by MogA, MoeA, MobA, and MobB, which is also in charge with the delivery of the mature cofactor onto the aponitrate reductase A in a NarJ-assisted process.

Received for publication, June 24, 2004 , and in revised form, July 8, 2004.

^* This work was supported by a grant from the Centre National de la Recherche Scientifique. 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.

Both authors have contributed equally to this work.

Supported by a Ministere Recherche Technologie fellowship.

^¶ Current address: LBME, CNRS, 118, route de Narbonne, 31062 Toulouse, France.

^|| To whom correspondence should be addressed. Tel.: 33-491-164-148; Fax: 33-491-718-914; E-mail: magalon{at}ibsm.cnrs-mrs.fr.

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