Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex
Abstract
The dynamic assembly and remodelling of eukaryotic chromosomes facilitate fundamental cellular processes such as DNA replication and gene transcription. The repeating unit of eukaryotic chromosomes is the nucleosome core, consisting of DNA wound about a defined octamer of histone proteins. Two enzymatic processes that regulate transcription by targeting elements of the nucleosome include ATP-dependent nucleosome remodelling and reversible histone acetylation. The histone deacetylases, however, are unable to deacetylate oligonucleosomal histones in vitro. The protein complexes that mediate ATP-dependent nucleosome remodelling and histone acetylation/deacetylation in the regulation of transcription were considered to be different, although it has recently been suggested that these activities might be coupled. We report here the identification and functional characterization of a novel ATP-dependent nucleosome remodelling activity that is part of an endogenous human histone deacetylase complex. This activity is derived from the CHD3 and CHD4 proteins which contain helicase/ATPase domains found in SWI2-related chromatin remodelling factors, and facilitates the deacetylation of oligonucleosomal histones in vitro. We refer to this complex as the nucleosome remodelling and deacetylating (NRD) complex. Our results establish a physical and functional link between the distinct chromatin-modifying activities of histone deacetylases and nucleosome remodelling proteins.
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mSin3A, SMRT, and N-CoR are part of large histone deacetylase complexes.
“The last three factors are part of the large histone deacetylase complexes (20, 51, 60).”
From Gamma Interferon Triggers Interaction between ICSBP (IRF-8) and TEL, Recruiting the Histone Deacetylase HDAC3 to the Interferon-Responsive Element (2002) · cites this paper as [51]
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Self-citation
- Authors
- Tong, J. K., Hassig, C. A., Schnitzler, G. R., Kingston, R. E., & Schreiber, S. L.
- Affiliations
- Howard Hughes Medical Institute (US)
- Massachusetts General Hospital (US)
- Corresponding author
- Schreiber, Stuart L.
- Venue
- Nature
- Published
- 1998-10
- Volume
- 395
- Issue
- 6705
- Pages
- 917-921
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1525573602
- Cited by
- 692
- References
- 15
- Citations by year
- 2026: 17 · 2025: 20 · 2024: 12 · 2023: 26 · 2022: 14 · 2021: 17 · 2020: 19 · 2019: 20 · 2018: 13 · 2017: 21 · 2016: 21 · 2015: 25 · 2014: 40 · 2013: 24 · 2012: 25
- FWCI
- 13.56
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Keywords
- chromatin deacetylation, histone deacetylase, nucleosome remodeling, CHD3, CHD4, histone acetylation, transcriptional regulation, histone deacetylase complex
- MeSH terms
- Acetylation, Adenosine Triphosphatases, Adenosine Triphosphate, Amino Acid Sequence, Autoantigens, Chromatin, DNA Helicases, HeLa Cells, Histone Deacetylases, Humans, Molecular Sequence Data, Multienzyme Complexes, Nucleosomes, Jurkat Cells, Macromolecular Substances, Mi-2 Nucleosome Remodeling and Deacetylase Complex
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