Sds3 (Suppressor of Defective Silencing 3) Is an Integral Component of the Yeast Sin3·Rpd3 Histone Deacetylase Complex and Is Required for Histone Deacetylase Activity
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SDS3 (suppressor of defective silencing 3) was originally identified in a screen for mutations that cause increased silencing of a crippled HMR silencer in a rap1 mutant background. In addition, sds3 mutants have phenotypes very similar to those seen in sin3 and rpd3 mutants, suggesting that it functions in the same genetic pathway. In this manuscript we demonstrate that Sds3p is an integral subunit of a previously identified high molecular weight Rpd3p.Sin3p containing yeast histone deacetylase complex. By analyzing an sds3Delta strain we show that, in the absence of Sds3p, Sin3p can be chromatographically separated from Rpd3p, indicating that Sds3p promotes the integrity of the complex. Moreover, the remaining Rpd3p complex in the sds3Delta strain had little or no histone deacetylase activity. Thus, Sds3p plays important roles in the integrity and catalytic activity of the Rpd3p.Sin3p complex.
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HDACs 1, 2 and 3 require association with large multisubunit corepressor complexes for maximal activity.
“HDACs 1, 2 and 3 require association with large multisubunit corepressor complexes for maximal activity7-12.”
From Structure of Hdac3 Bound to Co-Repressor and Inositol Tetraphosphate (2012) · cites this paper as [9]
The introduction (page unavailable) describes HDACs as multiprotein complexes associated with repressors and corepressors. The Discussion (page unavailable) reports that a yeast Rpd3p complex loses deacetylase activity when Sds3p is absent. The paper does not establish that HDACs 1, 2, and 3 each require such complexes for maximal activity. (LLM, conf=0.84)
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- Authors
- Lechner, T., Carrozza, M. J., Yu, Y., Grant, P. A., Eberharter, A., Vannier, D., Brosch, G., Stillman, D. J., Shore, D., & Workman, J. L.
- Affiliations
- Pennsylvania State University (US)
- University of Utah (US)
- Columbia University (US)
- Innsbruck Medical University (AT)
- University of Geneva (CH)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-12
- Volume
- 275
- Issue
- 52
- Pages
- 40961-40966
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2166899684
- Cited by
- 97
- References
- 42
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 4 · 2023: 5 · 2021: 2 · 2020: 3 · 2019: 3 · 2018: 5 · 2017: 1 · 2016: 3 · 2015: 3 · 2014: 2 · 2013: 1 · 2012: 3
- FWCI
- 1.57
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Archive ouverte UNIGE (University of Geneva) (publishedVersion, other-oa)
- Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
- Funders
- American Cancer Society
- Austrian Science Fund
- National Institute of General Medical Sciences
- 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 › Nuclear Structure and Function
- Keywords
- Sin3, Rpd3, histone deacetylase complex, histone deacetylase activity, silencing, Rap1, Saccharomyces cerevisiae
- MeSH terms
- Fungal Proteins, Histone Deacetylases, Repressor Proteins, Transcription Factors, Gene Silencing, Saccharomyces cerevisiae Proteins
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