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J. Biol. Chem., Vol. 282, Issue 29, 20804-20808, July 20, 2007

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Acetylated Histone Tail Peptides Induce Structural Rearrangements in the RSC Chromatin Remodeling Complex^*

From the Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115

Post-translational acetylation of histone tails is often required for the recruitment of ATP-dependent chromatin remodelers, which in turn mobilize nucleosomes on the chromatin fiber. Here we show that the lower lobe of the ATP-dependent chromatin remodeler RSC exists in a dynamic equilibrium and can be found extended away or retracted against the tripartite upper lobe of the complex. Extension of the lower lobe increases the size of a central cavity that has been proposed to be the nucleosome binding site. We show that the presence of acetylated histone 3 N-terminal tail peptides stabilizes the lower lobe of RSC in the retracted state, suggesting that domains recognizing the acetylated histone tails reside at the interface between the two lobes. Based on three-dimensional reconstructions, we propose a model for the interaction of RSC with acetylated nucleosomes.

Received for publication, April 27, 2007 , and in revised form, May 21, 2007.

^* 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.

The on-line version of this article (available at http://www.jbc.org) contains eight supplemental figures.

¹ A Damon Runyon Fellow, supported by the Damon Runyon Cancer Research Foundation (Grant DRG-1824-04).

² To whom correspondence should be addressed: Dept. of Cell Biology, Harvard Medical School, 240 Longwood Ave., Boston, MA 02115. Tel.: 617-432-4090; Fax: 617-432-1144; E-mail: twalz{at}hms.harvard.edu.