The HSA domain of BRG1 mediates critical interactions required for glucocorticoid receptor-dependent transcriptional activation in vivo.

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 the glucocorticoid receptor. We identified a domain within the N terminus of BRG1 that 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 mouse mammary tumor virus 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.
Mesh Terms:
Animals, Chromatin Assembly and Disassembly, Chromosomal Proteins, Non-Histone, DNA Helicases, Humans, Mammary Tumor Virus, Mouse, Mice, Mutant Proteins, Nuclear Proteins, Promoter Regions, Genetic, Protein Binding, Protein Structure, Tertiary, Protein Subunits, Receptors, Glucocorticoid, Sequence Deletion, Structure-Activity Relationship, Transcription Factors, Transcriptional Activation
Mol. Cell. Biol.
Date: Feb. 01, 2008
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