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
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
Cell
Date: May. 02, 1997
PubMed ID: 9150135
View in: Pubmed Google Scholar
Download Curated Data For This Publication
10254
Switch View:
- Interactions 4