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Molecular and Cellular Biology, May 2009, p. 2532-2545, Vol. 29, No. 10
0270-7306/09/$08.00+0     doi:10.1128/MCB.01682-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Mutational Analysis of the Sir3 BAH Domain Reveals Multiple Points of Interaction with Nucleosomes{triangledown}

Vinaya Sampath,1,§ Peihua Yuan,1,§,{dagger} Isabel X. Wang,1,# Evelyn Prugar,1 Fred van Leeuwen,2 and Rolf Sternglanz1*

Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York,1 Netherlands Cancer Institute, Amsterdam, The Netherlands2

Received 29 October 2008/ Returned for modification 28 November 2008/ Accepted 2 March 2009

Sir3, a component of the transcriptional silencing complex in the yeast Saccharomyces cerevisiae, has an N-terminal BAH domain that is crucial for the protein's silencing function. Previous work has shown that the N-terminal alanine residue of Sir3 (Ala2) and its acetylation play an important role in silencing. Here we show that the silencing defects of Sir3 Ala2 mutants can be suppressed by mutations in histones H3 and H4, specifically, by H3 D77N and H4 H75Y mutations. Additionally, a mutational analysis demonstrates that three separate regions of the Sir3 BAH domain are important for its role in silencing. Many of these BAH mutations also can be suppressed by the H3 D77N and H4 H75Y mutations. In agreement with the results of others, in vitro experiments show that the Sir3 BAH domain can interact with partially purified nucleosomes. The silencing-defective BAH mutants are defective for this interaction. These results, together with the previously characterized interaction between the C-terminal region of Sir3 and the histone H3/H4 tails, suggest that Sir3 utilizes multiple domains to interact with nucleosomes.

* Corresponding author. Mailing address: Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, NY 11794-5215. Phone: (631) 632-8565. Fax: (631) 632-8575. E-mail: rolf{at}life.bio.sunysb.edu

{triangledown} Published ahead of print on 9 March 2009.

§ These authors contributed equally to the work.

{dagger} Present address: Department of Cell and Developmental Biology, University of North Carolina, Chapel Hill, NC 27599.

# Present address: Abramson Research Center, University of Pennsylvania, Philadelphia, PA 19104.

Molecular and Cellular Biology, May 2009, p. 2532-2545, Vol. 29, No. 10
0270-7306/09/$08.00+0     doi:10.1128/MCB.01682-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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