The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
Histone Deacetylases and SAP18, a Novel Polypeptide, Are Components of a Human Sin3 Complex
Open accessAbstract
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.
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“RBBP4 and RBBP7 are present in many protein complexes other than the NuRD complex (Sin3 complex, PRC2), which also could explain their observed dynamic behavior [21,22].”
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Histone acetylation in chromatin structure and transcription
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Activation of p53 Sequence-Specific DNA Binding by Acetylation of the p53 C-Terminal Domain
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The coregulator exchange in transcriptional functions of nuclear receptors
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Twenty-Five Years of the Nucleosome, Fundamental Particle of the Eukaryote Chromosome
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Metadata
- Authors
- Zhang, Y., Iratni, R., Erdjument-Bromage, H., Tempst, P., & Reinberg, D.
- Affiliations
- Howard Hughes Medical Institute (US)
- Memorial Sloan Kettering Cancer Center (US)
- Corresponding author
- Reinberg, Danny
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1997-05
- Volume
- 89
- Issue
- 3
- Pages
- 357-364
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2074096799
- Cited by
- 578
- References
- 44
- Citations by year
- 2026: 6 · 2025: 10 · 2024: 10 · 2023: 14 · 2022: 8 · 2021: 14 · 2020: 14 · 2019: 11 · 2018: 10 · 2017: 8 · 2016: 15 · 2015: 11 · 2014: 18 · 2013: 14 · 2012: 6
- FWCI
- 19.00
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (2r01gm048518-05)
- National Cancer Institute (5P309CA08748)
- National Institute of General Medical Sciences (GM37120, GM-48518)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Keywords
- histone deacetylase, HDAC1, HDAC2, SAP18, SAP30, transcriptional repression, histone deacetylation, histone modifications, protein-protein interaction, core histones, transcriptional repressor
- MeSH terms
- Animals, Carrier Proteins, Cell Fractionation, HeLa Cells, Histone Deacetylases, Humans, Mammals, Molecular Sequence Data, Multienzyme Complexes, Nuclear Proteins, Precipitin Tests, Repressor Proteins, Retinoblastoma, Transcription Factors, Transcription, Genetic, Blotting, Western, RNA-Binding Proteins, Sequence Homology, Amino Acid, Saccharomyces cerevisiae Proteins, Retinoblastoma-Binding Protein 4, Retinoblastoma-Binding Protein 7, Co-Repressor Proteins
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