Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression.
Transcriptional repression by Mad-Max heterodimers requires interaction of Mad with the corepressors mSin3A/B. Sin3p, the S. cerevisiae homolog of mSin3, functions in the same pathway as Rpd3p, a protein related to two recently identified mammalian histone deacetylases, HDAC1 and HDAC2. Here, we demonstrate that mSin3A and HDAC1/2 are associated in ... vivo. HDAC2 binding requires a conserved region of mSin3A capable of mediating transcriptional repression. In addition, Mad1 forms a complex with mSin3 and HDAC2 that contains histone deacetylase activity. Trichostatin A, an inhibitor of histone deacetylases, abolishes Mad repression. We propose that Mad-Max functions by recruiting the mSin3-HDAC corepressor complex that deacetylates nucleosomal histones, producing alterations in chromatin structure that block transcription.
Mesh Terms:
Animals, Cells, Cultured, DNA-Binding Proteins, Gene Expression Regulation, Enzymologic, Histone Deacetylases, Multienzyme Complexes, Protein Binding, Protein Structure, Tertiary, Rabbits, Repressor Proteins, Saccharomyces cerevisiae Proteins, Transcription Factors, Transcription, Genetic
Animals, Cells, Cultured, DNA-Binding Proteins, Gene Expression Regulation, Enzymologic, Histone Deacetylases, Multienzyme Complexes, Protein Binding, Protein Structure, Tertiary, Rabbits, Repressor Proteins, Saccharomyces cerevisiae Proteins, Transcription Factors, Transcription, Genetic
Cell
Date: May. 02, 1997
PubMed ID: 9150134
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