Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex

Yi Zhang, Rabah Iratni, Hediye Erdjument-Bromage, Paul Tempst, Danny Reinberg

Research output: Contribution to journalArticlepeer-review

498 Citations (Scopus)

Abstract

An important event in gene expression is the covalent modification of histone proteins. We have found that the mammalian transcriptional repressor Sin3 (mSin3) exists in a complex with histone deacetylases HDAC1 and HDAC2. Consistent with the observation that mSin3-mediated repression of transcription involves the modification of histone polypeptides, we found that the mSin3-containing complex includes polypeptides that tether the mSin3 complex to core histone proteins. In addition, two novel mSin3-associated polypeptides, SAP18 and SAP30, were identified. We isolated a cDNA encoding human SAP18 and found that SAP18 is a component of an mSin3-containing complex in vivo. Moreover, we demonstrate a direct interaction between SAP18 and mSin3. SAP18 represses transcription in vivo when tethered to the promoter, consistent with the ability of SAP18 to interact with mSin3.

Original languageEnglish
Pages (from-to)357-364
Number of pages8
JournalCell
Volume89
Issue number3
DOIs
Publication statusPublished - May 2 1997
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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