Cited by 578Genomics and Chromatin DynamicsHistone Deacetylase Inhibitors ResearchEpigenetics and DNA Methylation

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Histone Deacetylases and SAP18, a Novel Polypeptide, Are Components of a Human Sin3 Complex

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Zhang, Yi, Iratni, Rabah, Erdjument-Bromage, Hediye, Tempst, Paul, Reinberg, Danny·1997·Cell

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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.

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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
ORCID: Zhang, Yi
Iratni, Rabah
Tempst, Paul
Reinberg, Danny
Venue: Cell
Publisher: Elsevier BV
Published: 1997-05
Volume: 89
Issue: 3
Pages: 357-364
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/s0092-8674(00)80216-0
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: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 5921 d)
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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Histone Deacetylases and SAP18, a Novel Polypeptide, Are Components of a Human Sin3 Complex

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