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

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.

Pubmed ID: 9150135

Authors

  • Zhang Y
  • Iratni R
  • Erdjument-Bromage H
  • Tempst P
  • Reinberg D

Journal

Cell

Publication Data

May 2, 1997

Associated Grants

  • Agency: NCI NIH HHS, Id: 5P309CA08748
  • Agency: NIGMS NIH HHS, Id: GM-37120
  • Agency: NIGMS NIH HHS, Id: GM-48518

Mesh Terms

  • Animals
  • Blotting, Western
  • Carrier Proteins
  • Cell Fractionation
  • HeLa Cells
  • Histone Deacetylases
  • Humans
  • Mammals
  • Molecular Sequence Data
  • Multienzyme Complexes
  • Nuclear Proteins
  • Precipitin Tests
  • Repressor Proteins
  • Retinoblastoma
  • Retinoblastoma-Binding Protein 4
  • Retinoblastoma-Binding Protein 7
  • Saccharomyces cerevisiae Proteins
  • Sequence Homology, Amino Acid
  • Transcription Factors
  • Transcription, Genetic