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J. Biol. Chem., Vol. 277, Issue 50, 48199-48204, December 13, 2002
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From the Laboratoire de Chimie Bactérienne, Institut Biologie
Structurale et Microbiologie, CNRS, 31 chemin Joseph Aiguier,
13402 Marseille cedex 09, France
The final stages of bacterial molybdenum cofactor
(Moco) biosynthesis correspond to molybdenum chelation and nucleotide
attachment onto an unique and ubiquitous structure, the molybdopterin.
Using a bacterial two-hybrid approach, here we report on the in
vivo interactions between MogA, MoeA, MobA, and MobB implicated
in several distinct although linked steps in Escherichia
coli. Numerous interactions among these proteins have been
identified. Somewhat surprisingly, MobB, a GTPase with a yet unclear
function, interacts with MogA, MoeA, and MobA. Probing the effects of
various mo. mutations on the interaction map allowed us (i)
to distinguish Moco-sensitive interactants from insensitive ones
involving MobB and (ii) to demonstrate that molybdopterin is a key
molecule triggering or facilitating MogA-MoeA and MoeA-MobA
interactions. These results suggest that, in vivo,
molybdenum cofactor biosynthesis occurs on protein complexes rather
than by the separate action of molybdenum cofactor biosynthetic proteins.
In Vivo Interactions between Gene Products Involved
in the Final Stages of Molybdenum Cofactor Biosynthesis in
Escherichia coli*
,
*
This work was supported by a grant from the Fondation pour
la Recherche Médicale (to A. M.) and by the CNRS.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 33-4-91164148;
Fax: 33-4-91718914; E-mail: magalon@ibsm.cnrs-mrs.fr.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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