Abstract
Transcriptional repression by nuclear receptors has been correlated to binding of the putative co-repressor, N-CoR. A complex has been identified that contains N-CoR, the Mad presumptive co-repressor mSin3, and the histone deacetylase mRPD3, and which is required for both nuclear receptor- and Mad-dependent repression, but not for repression by transcription factors of the ets-domain family. These data predict that the ligand-induced switch of heterodimeric nuclear receptors from repressor to activator functions involves the exchange of complexes containing histone deacetylases with those that have histone acetylase activity.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
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Binding Sites
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Cell Line
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DNA-Binding Proteins / physiology
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Gene Expression Regulation*
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HeLa Cells
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Histone Deacetylases / physiology*
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Humans
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Nuclear Proteins / physiology*
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Nuclear Receptor Co-Repressor 1
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Protein Binding
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Rats
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Receptors, Cytoplasmic and Nuclear / physiology
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Receptors, Thyroid Hormone / genetics
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Repressor Proteins / physiology*
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Saccharomyces cerevisiae Proteins*
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Transcription Factors / physiology*
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Transcription, Genetic
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Transfection
Substances
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Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
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DNA-Binding Proteins
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MXD1 protein, human
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NCOR1 protein, human
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Ncor1 protein, rat
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Nuclear Proteins
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Nuclear Receptor Co-Repressor 1
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Receptors, Cytoplasmic and Nuclear
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Receptors, Thyroid Hormone
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Recombinant Fusion Proteins
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Repressor Proteins
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SIN3 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Transcription Factors
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Histone Deacetylases