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Molecular and Cellular Biology, June 2002, p. 3653-3662, Vol. 22, No. 11
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.11.3653-3662.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Nucleosome Remodeling by the Human SWI/SNF Complex Requires Transient Global Disruption of Histone-DNA Interactions

Sayura Aoyagi,1 Geeta Narlikar,2,3 Chunyang Zheng,1 Saïd Sif,2,3,{dagger} Robert E. Kingston,2,3 and Jeffrey J. Hayes1*

Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, New York 14642,1 Department of Molecular Biology, Massachusetts General Hospital, Boston, Massachusetts 02114,2 Department of Genetics, Harvard Medical School, Boston, Massachusetts 021153

Received 18 January 2002/ Accepted 27 February 2002

We utilized a site-specific cross-linking technique to investigate the mechanism of nucleosome remodeling by hSWI/SNF. We found that a single cross-link between H2B and DNA virtually eliminates the accumulation of stably remodeled species as measured by restriction enzyme accessibility assays. However, cross-linking the histone octamer to nucleosomal DNA does not inhibit remodeling as monitored by DNase I digestion assays. Importantly, we found that the restriction enzyme-accessible species can be efficiently cross-linked after remodeling and that the accessible state does not require continued ATP hydrolysis. These results imply that the generation of stable remodeled states requires at least transient disruption of histone-DNA interactions throughout the nucleosome, while hSWI/SNF-catalyzed disruption of just local histone-DNA interactions yields less-stable remodeled states that still display an altered DNase I cleavage pattern. The implications of these results for models of the mechanism of SWI/SNF-catalyzed nucleosome remodeling are discussed.

* Corresponding author. Mailing address: Department of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, NY 14642. Phone: (716) 273-4887. Fax: (716) 271-2683. E-mail: jjhs{at}uhura.cc.rochester.edu.

{dagger} Present address: Department of Molecular and Cellular Biochemistry, Ohio State University, Columbus, OH 43210.

Molecular and Cellular Biology, June 2002, p. 3653-3662, Vol. 22, No. 11
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.11.3653-3662.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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