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Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression

C D Laherty1, W M Yang, J M Sun

  • 1Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98104, USA.

Cell
|May 2, 1997
PubMed

Insights

Mad-Max proteins recruit mSin3-HDAC complexes to repress transcription. This complex deacetylates histones, altering chromatin structure and blocking gene expression, a process inhibited by Trichostatin A.

Area of Science:

  • Molecular Biology
  • Epigenetics
  • Gene Regulation

Background:

  • Mad-Max heterodimers mediate transcriptional repression.
  • Corepressors mSin3A/B interact with Mad proteins.
  • Histone deacetylases (HDACs) are crucial in chromatin regulation.

Purpose of the Study:

  • To investigate the interaction between mSin3A, HDAC1/2, and Mad proteins.
  • To elucidate the mechanism of Mad-Max-mediated transcriptional repression.

Main Methods:

  • In vivo association studies.
  • Analysis of protein complex formation.
  • Assessment of histone deacetylase activity.
  • Inhibition studies using Trichostatin A.

Main Results:

  • mSin3A and HDAC1/2 were found to be associated in vivo.
  • HDAC2 binding to mSin3A depends on a specific conserved region.
  • Mad1 forms a complex with mSin3 and HDAC2 possessing histone deacetylase activity.
  • Trichostatin A inhibited Mad-mediated repression.

Conclusions:

  • Mad-Max functions by recruiting the mSin3-HDAC corepressor complex.
  • This complex deacetylates nucleosomal histones.
  • Alterations in chromatin structure induced by deacetylation lead to transcriptional blocking.

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