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.
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
Date: May. 02, 1997
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