Rest repression of neuronal genes requires components of the hSWI·SNF complex

Battaglioli, E; Andres, M. E.; Chenoweth J.G.; Anderson M.E.; Mandel, G; Rose D.W.; Rosenfeld M.G.

Keywords: sequence, acid, proteins, system, neurons, rat, enzyme, dna, glutathione, fluorescence, animals, expression, antibody, transcription, regions, complex, genes, rats, protein, cell, gene, channel, antibodies, electrophoresis, chain, immunoprecipitation, channels, microscopy, line, humans, chromatin, human, gel, polymerase, regulation, sodium, nerve, biochemistry, tissue, formation, adenosine, molecular, data, article, factor, promoter, hybrid, activity, techniques, controlled, repressor, deacetylase, animal, histone, polyacrylamide, factors, study, neurology, amino, priority, Reaction, nonhuman, journal, Animalia, Homology,, triphosphatase, Immunoblotting, (Genetics), transferase, alternative, splicing, chromosomal, Proteins,, Non-Histone, Deacetylation, Deacetylases, Two-Hybrid


A function of the transcription factor REST is to block the expression of neuronal phenotypic traits in nonneuronal cells. Previous studies have shown that REST-mediated repression requires histone deacetylase activity and that recruitment of deacetylases is mediated by two co-repressors, Sin3A and CoREST. In this study, we show that a repressor domain in CoREST interacts with BRG1-associated factor (BAF) 57, a component of the hSWI·SNF complex. In vivo, BAF57 occupies the neuronal sodium channel gene (Nav1.2) promoter, and targeting to this gene requires REST. In addition to BAF57, the ATPase BRG1 and BAF170, other members of the hSWI·SNF complex, are also present in the REST·CoREST repressor complex. Microinjection of specific antibodies against BRG1, BAF57, or BAF170 into Rat1 fibroblasts relieves repression of RE1 reporter genes. Together, our data suggest that ATP-dependent chromatin remodeling, as well as histone deacetylation, is needed for REST-mediated repression.

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Título según SCOPUS: Rest repression of neuronal genes requires components of the hSWI·SNF complex
Volumen: 277
Número: 43
Editorial: Elsevier
Fecha de publicación: 2002
Página de inicio: 41038
Página final: 41045
Idioma: English