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PMID: 17023429 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

BRG1 chromatin remodeling activity is required for efficient chromatin binding by repressor element 1-silencing transcription factor (REST) and facilitates REST-mediated repression.

The Journal of biological chemistry ·Vol. 281 ·No. 51 ·2006-12-22 ·Pages 38974-80

Ooi L, Belyaev ND, Miyake K, Wood IC, Buckley NJ

Abstract

Chromatin remodeling enzymes such as SWI/SNF use the hydrolysis of ATP to power the movement of nucleosomes with respect to DNA. BRG1, one of the ATPases of the SWI/SNF complex, can be recruited by both activators and repressors, although the precise role of BRG1 in mechanisms of repression has thus far remained unclear. One transcription factor that recruits BRG1 as a corepressor is the repressor element 1-silencing transcription factor (REST). Here we address for the first time the mechanism of BRG1 activity in gene repression. We found that BRG1 enhanced REST-mediated repression at some REST target genes by increasing the interaction of REST with the local chromatin at its binding sites. Furthermore, REST-chromatin interactions, mediated by BRG1, were enhanced following an increase in histone acetylation in a manner dependent on the BRG1 bromodomain. Our data suggest that BRG1 facilitates REST repression by increasing the interaction between REST and chromatin. Such a mechanism may be applicable to other transcriptional repressors that utilize BRG1.

MeSH Terms
Acetylation Adenosine Triphosphate/chemistry Binding Sites Cell Line Cell Nucleus/metabolism Chromatin/chemistry DNA Helicases/chemistry,physiology Histones/chemistry Humans Hydroxamic Acids/pharmacology Nuclear Proteins/chemistry,physiology Plasmids/metabolism Protein Binding Repressor Proteins/chemistry,physiology Transcription Factors/chemistry,physiology Transcription, Genetic Transfection
Chemicals
Chromatin Histones Hydroxamic Acids Nuclear Proteins RE1-silencing transcription factor Repressor Proteins Transcription Factors trichostatin A Adenosine Triphosphate SMARCA4 protein, human DNA Helicases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Ooi Lezanne
Institute of Membrane and Systems Biology, University of Leeds, Leeds LS2 9JT, United Kingdom. [email protected]
Belyaev Nikolai D
Miyake Katsuhide
Wood Ian C
Buckley Noel J
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Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
2006-12-22
Epub
2006-00-04
Pages
38974-80
Language
English
Region
United States
NLM ID
2985121R
PMCID
PMC1820614
Subset
IM
Grants
Wellcome Trust · United Kingdom
Wellcome Trust · 075168 · United Kingdom
Wellcome Trust · 076391 · United Kingdom
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