Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex Journal Article
| Authors: | Zhang, Y.; Iratni, R.; Erdjument-Bromage, H.; Tempst, P.; Reinberg, D. |
| Article Title: | Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex |
| 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. |
| Keywords: | controlled study; dna binding protein; human cell; promoter region; mammalia; animals; complex formation; transcription factor; transcription, genetic; retinoblastoma; enzyme activity; hela cells; transcription factors; nuclear proteins; gene activation; blotting, western; transcription regulation; amino acid sequence; molecular sequence data; sequence homology, amino acid; histone; gene repression; carrier proteins; immunoblotting; cell fractionation; saccharomyces cerevisiae proteins; multienzyme complexes; mammals; repressor proteins; histone deacetylases; histone deacetylase; acetylation; polypeptide; affinity chromatography; precipitin tests; humans; human; priority journal; article |
| Journal Title: | Cell |
| Volume: | 89 |
| Issue: | 3 |
| ISSN: | 0092-8674 |
| Publisher: | Cell Press |
| Date Published: | 1997-05-02 |
| Start Page: | 357 |
| End Page: | 364 |
| Language: | English |
| DOI: | 10.1016/s0092-8674(00)80216-0 |
| PUBMED: | 9150135 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 17 March 2017 -- Source: Scopus |
