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J. Biol. Chem., Vol. 279, Issue 41, 42374-42382, October 8, 2004

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The Histone Octamer Is Invisible When NF-B Binds to the Nucleosome^*

Dimitar Angelov¶, François Lenouvel, Fabienne Hans, Christoph W. Müller||, Philippe Bouvet, Jan Bednar**, Evangelos N. Moudrianakis, Jean Cadet, and Stefan Dimitrov¶¶

From the Laboratoire de Biologie Moléculaire et Cellulaire de la Différenciation, INSERM U309, Institut Albert Bonniot, Domaine de la Merci, 38706 La Tronche Cedex, France, the ^||European Molecular Biology Laboratory, Grenoble Outstation, BP 181, 38042 Grenoble Cedex 9, France, Ecole Normale Supérieure de Lyon, CNRS-Unité Mixte de Recherche 5161, 46 Allée d'Italie, 69007 Lyon, France, ^**CNRS, Laboratoire Spectrometrie Physique, BP87, 38402 St. Martin d'Heres Cedex, France, the Departments of Biology and Biophysics, The Johns Hopkins University, Baltimore, Maryland 21218, and Commissariat à l'Energie Atomique/Département de Recherche Fondamentale sur la Matière Condensée, SCIB/LAN, F-38054 Grenoble Cedex 9, France

The transcription factor NF-B is involved in the transcriptional control of more than 150 genes, but the way it acts at the level of nucleosomal templates is not known. Here we report on a study examining the interaction of NF-B p50 with its DNA recognition sequence in a positioned nucleosome. We demonstrate that NF-B p50 was able to bind to the nucleosome with an apparent association constant close to that for free DNA. In agreement with this, the affinity of NF-B p50 binding does not depend on the localization of its recognition sequence relative to the nucleosome dyad axis. In addition, the binding of NF-B p50 does not induce eviction of histones and does not perturb the overall structure of the nucleosome. The NF-B p50-nucleosome complex exhibits, however, local structural alterations within the NF-B p50 recognition site. Importantly, these alterations were very similar to those found in the NF-B p50-DNA complex. Our data suggest that NF-B p50 can accommodate the distorted, bent DNA within the nucleosome. This peculiar property of NF-B p50 might have evolved to meet the requirements for its function as a central switch for stress responses.

Received for publication, June 28, 2004 , and in revised form, July 19, 2004.

^* This work was supported by grants from CNRS and INSERM (to S. D.), grants from Région Rhône Alpes, ATIP CNRS (to P. B.), and National Science Foundation Grant BG K902 and NATO CLG 976174 (to D. A.). 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.

^¶ Supported by visiting scientist fellowships from the Commissariat à l'Energie Atomique and the Région Rhône Alpes while on leave from the Institute of Solid State Physics, Bulgarian Academy of Sciences, Sofia, Bulgaria. To whom correspondence may be addressed. Tel.: (33)-4-76-54-94-73; Fax: (33)-4-76-54-95-95.

^¶¶ To whom correspondence may be addressed. Tel.: (33)-4-76-54-94-73; Fax: (33)-4-76-54-95-95; E-mail: stefan.dimitrov{at}ujf-grenoble.fr.

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