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. 1997 May 2;89(3):349-56.
doi: 10.1016/s0092-8674(00)80215-9.

Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression

C D Laherty  1 , W M Yang, J M Sun, J R Davie, E Seto, R N Eisenman
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Free article

Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression

C D Laherty et al. Cell. .
Free article

Abstract

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.

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