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J. Biol. Chem., Vol. 278, Issue 49, 48590-48601, December 5, 2003

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Linker Histone H1 Modulates Nucleosome Remodeling by Human SWI/SNF^*

Aruna Ramachandran, Mahera Omar, Peter Cheslock, and Gavin R. Schnitzler¶

From the Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111

Chromatin, a combination of nucleosomes and linker histones, inhibits transcription by blocking polymerase movement and access of factors to DNA. ATP-dependent remodeling complexes such as SWI/SNF and RSC alter chromatin structure to increase or decrease this repression. To further our understanding of how human SWI/SNF (hSWI/SNF) "remodels" chromatin we examined the octamer location, nature, and template specificity of hSWI/SNF-remodeled mononucleosomes when free or bound by linker histone H1. We find that, in the absence of H1, hSWI/SNF consistently moves nucleosomes to DNA ends, regardless of template sequence. On some sequences the repositioned histone octamer appears to be moved 45 bp off the DNA edge, whereas on others it appears to be normal, suggesting that the nature of the remodeled nucleosome can be influenced by DNA sequence. By contrast, in the presence of histone H1, hSWI/SNF slides octamers to more central positions and does not promote nucleosome movement off the ends of the DNA. Our results indicate that the nature and position of hSWI/SNF products may be influenced both by DNA sequence and linker histone, and shed light on the roles of H1 and hSWI/SNF in modulating chromatin structure.

Received for publication, August 14, 2003 , and in revised form, September 22, 2003.

^* This work was supported by National Institutes of Health Grant K01CA88835, by The Medical Foundation (New Investigator award), and by the Biomedical Research Support Program of Howard Hughes Medical Institute (to G. R. S.). 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.

Present address: Printing House, 5th Floor, Daily Jang Bldg., I.I. Chundrigar Road, Karachi, Pakistan.

Present address: Dept. of Molecular Biology and Microbiology, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111.

^¶ To whom correspondence should be addressed: Tufts University School of Medicine, Biochemistry Dept., 136 Harrison Ave., Boston, MA 02111. Tel.: 617-636-2441; Fax: 617-636-2409; E-mail: gavin.schnitzler{at}tufts.edu.

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