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 RIS Download
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