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Originally published In Press as doi:10.1074/jbc.M205961200 on August 27, 2002

J. Biol. Chem., Vol. 277, Issue 44, 41674-41685, November 1, 2002
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Largest Subunits of the Human SWI/SNF Chromatin-remodeling Complex Promote Transcriptional Activation by Steroid Hormone Receptors*

Hiroko InoueDagger §, Takako FurukawaDagger §, Stavros GiannakopoulosDagger , Sharleen Zhou||, David S. King||, and Naoko TaneseDagger **

From the Dagger  Department of Microbiology and Kaplan Cancer Center, New York University School of Medicine, New York, New York 10016-6481 and the || Department of Molecular and Cell Biology, Howard Hughes Medical Institute, University of California, Berkeley, California 94720-3204

The mammalian SWI/SNF-related complexes facilitate gene transcription by remodeling chromatin using the energy of ATP hydrolysis. The recruitment of these complexes to promoters remains poorly understood and may involve histone modifications or direct interactions with site-specific transcription factors or other cofactors. Here we report the isolation of two related but distinct cDNA clones, hOsa1 and hOsa2, that encode the largest subunits of human SWI/SNF. hOsa1 is identical to previously reported BAF250, and hOsa2 shares a high degree of sequence similarity with hOsa1. Mass spectrometric analysis, and immunoblotting with antibodies specific to hOsa1 or hOsa2 demonstrate the presence of both proteins in SWI/SNF-A but not in the related polybromo-BRG1-associated factors complex purified from HeLa cells. Co-precipitation studies indicate that hOsa1 and hOsa2 associate with BRG1 and hBRM through the C-terminal domain of hOsa. We define multiple domains within hBRM and BRG1 that interact with the hOsa C terminus. In cultured mammalian cells, hOsa1 and hOsa2 stimulate transcription by the glucocorticoid, estrogen, and androgen receptors. The glucocorticoid receptor-mediated activation is not observed with the C-terminal domain or with the hOsa2 polypeptide lacking the ARID DNA binding domain. These results suggest that hOsa1 and hOsa2 participate in promoting transcriptional activation by the steroid hormone receptors.

* This work was supported in part by American Cancer Society Grant RSG-01-248-01-CCE. Computing Resources was supported by National Science Foundation Grant BIR-9318128.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF521670 and AF521671.

§ Both authors contributed equally to this work.

Present address: Biomedical Imaging Research Center, Fukui Medical University, Shimoaizuki, Matsuoka, Yoshida, Fukui 910-1193, Japan.

** Supported in part by the Irma T. Hirschl Trust. To whom correspondence should be addressed: NYU School of Medicine, Dept. of Microbiology, 550 First Ave., MSB-258, New York, NY 10016-6481. Tel.: 212-263-8945; Fax: 212-263-8276; E-mail: tanesn01@med.nyu.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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