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Originally published In Press as doi:10.1074/jbc.M206037200 on August 27, 2002

J. Biol. Chem., Vol. 277, Issue 44, 41657-41666, November 1, 2002
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The Degree of Oligomerization of the H-NS Nucleoid Structuring Protein Is Related to Specific Binding to DNA*

Cyril BadautDagger §, Roy WilliamsDagger , Véronique Arluison||**, Emeline BouffartiguesDagger Dagger , Bruno Robert||, Henri BucDagger , and Sylvie RimskyDagger Dagger Dagger §§

From the Dagger  URA 1773 du CNRS, Institut Pasteur, 25 Rue du Dr. Roux, 75724 Paris cedex 15, France, Dagger Dagger  Enzymologie et Cinétique Structurale, UMR 8532 Ecole Normale Supérieure de Cachan/CNRS, IGR, 39 Rue C. Desmoulins, 94805 Villejuif cedex, France, and || Section de Biophysique des Fonctions Membranaires, DBJC/CEA et URA CNRS 2096, Commissariat à l'Energie Atomique Saclay, 91191 Gif-sur-Yvette Cedex, France

At several E. coli promoters, initiation of transcription is repressed by a tight nucleoprotein complex formed by the assembly of the H-NS protein. In order to characterize the relationship between the structure of H-NS oligomers in solution and on relevant DNA fragments, we have compared wild-type H-NS and several transdominant H-NS mutants using gel shift assays, DNase I footprinting, analytical ultracentrifugation, and reactivity toward a cross-linking reagent. In solution, oligomerization occurs through two protein interfaces, one necessary to construct a dimeric core (and involving residues 1-64) and the other required for subsequent assembly of these dimers. We show that, as well as region 64-95, residues present in the NH2-terminal coiled coil domain also participate in this second interface. Our results support the view that the same interacting interfaces are also involved on the DNA. We propose that the dimeric core recognizes specific motifs, with the second interface being critical for their correct head to tail assembly. The COOH-terminal domain of the protein contains the DNA binding motif essential for the discrimination of this specific functional assembly over competitive nonspecific H-NS polymers.

* This work was supported by a "Program de Recherche en Biologie Fondamentale en Microbiologie et Maladies infectieuses" grant from the Ministère de l'Education Nacionale de la Recherche et de la Technologie (MNERT) and by a grant from Fondatíon pour la Recherche Médicale (FRM) supporting the creation of the "Enzymologie et cinétique structurale" group.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.

§ Present address: URA 2185 du CNRS/Unité d'Immunologie Structurale, Institut Pasteur, 25 rue du Dr. Roux 75724, Paris cedex 15, France.

Recipient of fellowships from FRM and MNERT.

** Supported by a postdoctoral fellowship from the Commissariat à l'Energie Atomique. Present address: IBPC, 13 rue P. et M. Curie, 75005 Paris, France.

§§ To whom correspondence should be addressed: IGR, 39 rue C. Desmoulins, 94805 Villejuif cedex, France. Tel.: 33-1-42-11-50-08; Fax: 33-1-42-11-52-76; E-mail: srimsky@igr.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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