Isolation of a novel histone deacetylase reveals that class I and class II deacetylases promote SMRT-mediated repression

Hung Ying Kao, Michael Downes, Peter Ordentlich, Ronald M. Evans

Research output: Contribution to journalArticlepeer-review

359 Citations (Scopus)

Abstract

The transcriptional corepressor SMRT functions by mediating the repressive effect of transcription factors involved in diverse signaling pathways. The mechanism by which SMRT represses basal transcription has been proposed to involve the indirect recruitment of histone deacetylase HDAC1 via the adaptor mSin3A. In contrast to this model, a two-hybrid screen on SMRT- interacting proteins resulted in the isolation of the recently described HDAC5 and a new family member termed HDAC7. Molecular and biochemical results indicate that this interaction is direct and in vivo evidence colocalizes SMRT, mHDAC5, and mHDAC7 to a distinct nuclear compartment. Surprisingly, HDAC7 can interact with mSin3A in yeast and in mammalian cells, suggesting association of multiple repression complexes. Taken together, our results provide the first evidence that SMRT-mediated repression is promoted by class I and class II histone deacetylases and that SMRT can recruit class II histone deacetylases in a mSin3A-independent fashion.

Original languageEnglish
Pages (from-to)55-66
Number of pages12
JournalGenes and Development
Volume14
Issue number1
Publication statusPublished - 2000 Jan 1

All Science Journal Classification (ASJC) codes

  • Genetics
  • Developmental Biology

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