Transcriptional activation domains of human heat shock factor 1 recruit human SWI/SNF.
Chromatin remodeling complexes such as SWI/SNF use the energy of ATP hydrolysis to remodel nucleosomal DNA and increase transcription of nucleosomal templates. Human heat shock factor one (hHSF1) is a tightly regulated activator that stimulates transcriptional initiation and elongation using different portions of its activation domains. Here we demonstrate that ... hHSF1 associates with BRG1, the ATPase subunit of human SWI/SNF (hSWI/SNF) at endogenous protein concentrations. We also show that hHSF1 activation domains recruit hSWI/SNF to a chromatin template in a purified system. Mutation of hHSF1 residues responsible for activation of transcriptional elongation has the most severe effect on recruitment of SWI/SNF and association of hHSF1 with BRG1, suggesting that recruitment of chromatin remodeling activity might play a role in stimulation of elongation.
Mesh Terms:
Binding Sites, Chromatin, DNA Helicases, DNA-Binding Proteins, Heat-Shock Proteins, Hela Cells, Humans, Nuclear Proteins, Recombinant Fusion Proteins, Templates, Genetic, Transcription Factors, Transcriptional Activation
Binding Sites, Chromatin, DNA Helicases, DNA-Binding Proteins, Heat-Shock Proteins, Hela Cells, Humans, Nuclear Proteins, Recombinant Fusion Proteins, Templates, Genetic, Transcription Factors, Transcriptional Activation
Mol. Cell. Biol.
Date: Sep. 01, 2001
PubMed ID: 11486022
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