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Mol. Cell. Biol. doi:10.1128/MCB.01301-07
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

The HSA Domain of BRG1 Mediates Critical Interactions Required for GR-dependent Transcriptional Activation in vivo

Laboratory of Molecular Carcinogenesis, NIEHS/NIH, Research Triangle Park, North Carolina 27709; Department of Molecular Biology, Massachusetts General Hospital, Boston, Massachusetts 02114; Department of Genetics, Harvard Medical School, Boston, Massachusetts 02115; and Division of Basic Science, Fox Chase Cancer Center, Philadelphia, PA 19111

^* To whom correspondence should be addressed. Email: archer1{at}niehs.nih.gov.

	Abstract

The packaging of eukaryotic DNA into chromatin can create an impediment to transcription by hindering binding of essential factors required for transcription. The mammalian SWI/SNF remodeling complex has been shown to alter local chromatin structure and facilitate recruitment of transcription factors. BRG1 (or hBrm), the central ATPase of the human SWI/SNF complex, is a critical factor for the functional activity of nuclear receptor complexes. Analysis using BRG1/SNF2h chimeras suggests BRG1 may contain previously uncharacterized functional motifs important for SWI/SNF. To identify these regions, BRG1 truncation and deletion mutants were designed, characterized, and utilized in a series of assays to evaluate transcriptional activation and chromatin remodeling by glucocorticoid receptor. We identified a domain within the N-terminus of BRG1 which mediates critical protein interactions within SWI/SNF. We find the HSA domain of BRG1 is required to mediate the interaction with BAF250a/ARID1A and show this association is necessary for transcriptional activation from chromatin MMTV or endogenous promoters in vivo. These studies suggest BAF250a is a necessary facilitator of BRG1 mediated chromatin remodeling required for SWI/SNF-dependent transcriptional activation.