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J. Biol. Chem., Vol. 280, Issue 20, 19958-19965, May 20, 2005

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Histone Octamer Instability under Single Molecule Experiment Conditions^*

Cyril Claudet, Dimitar Angelov¶||, Philippe Bouvet¶, Stefan Dimitrov¶**, and Jan Bednar

From the Laboratoire de Spectrometrie Physique, CNRS, UMR 5588, BP87, 140 Av. de la Physique, 38402 St. Martin d'Heres Cedex, France, Ecole Normale Supérieure de Lyon, CNRS-UMR 5161, 46 Allée d'Italie, 69007 Lyon, France, the ^**Laboratoire de Biologie Moléculaire et Cellulaire de la Différenciation, INSERM U309, Institut Albert Bonniot, Domaine de la Merci, 38706 La Tronche Cedex, France, ^¶Laboratoire de Recherche "Joliot Curie," Ecole Normale Supérieure de Lyon, 46 Allée d'Italie, 69007 Lyon, France

We have studied the sample concentration-dependent and external stress-dependent stability of native and reconstituted nucleosomal arrays. Whereas upon stretching a single chromatin fiber in a solution of very low chromatin concentration the statistical distribution of DNA length released upon nucleosome unfolding shows only one population centered around 25 nm, in nucleosome stabilizing conditions a second population with average length of 50 nm was observed. Using radioactively labeled histone H3 and H2B, we demonstrate that upon lowering the chromatin concentration to very low values, first the linker histones are released, followed by the H2A-H2B dimer, whereas the H3-H4 tetramer remains stably attached to DNA even at the lowest concentration studied. The nucleosomal arrays reconstituted on a 5 S rDNA tandem repeat exhibited similar behavior. This suggests that the 25-nm disruption length is a consequence of the histone H2A-H2B dimer dissociation from the histone octamer. In nucleosome stabilizing conditions, a full 145 bp is constrained in the nucleosome. Our data demonstrate that the nucleosome stability and histone octamer integrity can be severely degraded in experiments where the sample concentration is low.

Received for publication, January 5, 2005 , and in revised form, March 9, 2005.

^* This work was supported by CNRS, INSERM, Région Rhône-Alpes, and grants from the Ministère de la Recherche (ACI Biologie Cellulaire Moléculaire et Structurale, BCM0070, ACI Interface Physique-Chimie-Biologie: Dynamique et Réactivité des Assemblages Biologiques (DRAB), 2004, Grant 04 2 136) and by the CNRS Action Thématique et Incitative sur Programme subvention (to J. B.). 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.

^|| On leave from the Institute of Solid State Physics, BAS, Sofia, Bulgaria. Supported by the National Science Fund-Bulgaria and the Région Rhône-Alpes.

To whom correspondence should be addressed: CNRS, Laboratoire de Spectrometrie Physique, UMR 5588, BP87, 140 Av. de la Physique, 38402 St. Martin d'Heres Cedex, France. Tel.: 33-4-76514761; Fax: 33-4-76635495; E-mail: jbednar{at}spectro.ujf-grenoble.fr.

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