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J. Biol. Chem., Vol. 280, Issue 50, 41777-41783, December 16, 2005

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Effects of HMGN1 on Chromatin Structure and SWI/SNF-mediated Chromatin Remodeling^*

David A. Hill1, Craig L. Peterson, and Anthony N. Imbalzano

From the Department of Cell Biology at the University of Massachusetts Medical School, Worcester, Massachusetts 01655 and the Program in Molecular Medicine at the University of Massachusetts Medical School, Worcester, Massachusetts 01605

The dynamic modulation of chromatin structure is determined by many factors, including enzymes that modify the core histone proteins, enzymes that remodel the structure of chromatin, and factors that bind to genomic DNA to affect its structure. Previous work indicates that the nucleosome binding family of high mobility group proteins (HMGN) facilitates the formation of a chromatin structure that is more conducive for transcription. SWI/SNF complexes are ATP-dependent chromatin remodeling enzymes that alter nucleosome structure to facilitate the binding of various regulatory proteins to chromatin. Here we examine the structural consequences of reconstituting chromatin with HMGN1 and the resulting effects on hSWI/SNF function. We demonstrate that HMGN1 decreases the sedimentation velocity of nucleosomal arrays in low ionic strength buffers but has little effect on the structure of more highly folded arrays. We further demonstrate that HMGN1 does not affect SWI/SNF-dependent chromatin remodeling on either mononucleosomes or nucleosomal arrays, indicating that SWI/SNF functions independently of HMGN1.

Received for publication, September 1, 2005 , and in revised form, October 20, 2005.

^* This work was supported by American Cancer Society Fellowship GMC-100065 (to D. A. H.) and by NCI/National Institutes of Health Grant P01 CA82834 (to A. N. I. and C. L. P.). 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.

¹ To whom correspondence should be addressed: Dept. of Cell Biology, S3-209, University of Massachusetts Medical School, 55 Lake Ave. North, Worcester, MA 01655. Tel.: 508-856-1049; Fax: 508-856-5612; E-mail: david.hill{at}umassmed.edu.

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