Cited by 97Genomics and Chromatin DynamicsHistone Deacetylase Inhibitors ResearchNuclear Structure and Function

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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Lechner, Thomas, Carrozza, Michael J., Yu, Yaxin, Grant, Patrick A., Eberharter, Anton, Vannier, David, Brosch, Gerald, Stillman, David J. +2 more·2000·Journal of Biological Chemistry

Abstract

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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Crossref · 10.1074/jbc.m005730200

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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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Research works printed but not linked: 3

  1. Steger, D. J., Eberharter, A., John, S., Grant, P. A., and Workman, J. L. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 12924 -12929
  2. Rundlett, S. E., Carmen, A. A., Kobayashi, R., Bavykin, S., Turner, B. M., and Grunstein, M. (1996) Proc. Natl. Acad. Sci. U. S. A. 93, 14503-14508
  3. Carmen, A. A., Griffin, P. R., Calaycay, J. R., Rundlett, S. E., Suka, Y., and Grunstein, M. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 12356 -12361

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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
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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