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Originally published In Press as doi:10.1074/jbc.M005730200 on October 9, 2000

J. Biol. Chem., Vol. 275, Issue 52, 40961-40966, December 29, 2000
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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*

Thomas Lechnerab, Michael J. Carrozzaac, Yaxin Yud, Patrick A. Grantae, Anton Eberhartera, David Vannierf, Gerald Broschgh, David J. Stillmand, David Shorei, and Jerry L. Workmanaj

From the a Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802-4500, the d Division of Molecular Biology and Genetics, Department of Oncological Sciences, University of Utah Health Sciences Center, Salt Lake City, Utah 84132, the f Department of Microbiology, Columbia University, New York, New York 10032, the g Department of Microbiology, University of Innsbruck-Medical School, Innsbruck A-6020, Austria, and the i Department of Molecular Biology, University of Geneva, 30 quai Ernest-Ansermet, CH-1211 Geneva 4, Switzerland

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.

* This work was supported in part by a grant from the National Institute of General Medical Sciences (to J. L. W.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

b Supported by a fellowship from the Austrian Science Foundation (FWF).

c An Howard Hughes Medical Institute Postdoctoral Associate.

e Supported by Postdoctoral Fellowship PF-98-017-01-GMC from the American Cancer Society and by Burroughs Wellcome.

h Supported by an grant from the Austrian Academy of Science (APART fellowship).

j An Associate Investigator of Howard Hughes Medical Institute. To whom correspondence should be addressed: Howard Hughes Medical Institute, Dept. of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802-4500. Tel.: 814-863-8256; Fax: 814-863-0099; E-mail: jlw10@psu.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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