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

Mutational Analysis of the Sir3 BAH Domain Reveals Multiple Points of Interaction with Nucleosomes Mutational Analysis of the Sir3 BAH Domain Reveals Multiple Points of Interaction with Nucleosomes ▿ Vinaya Sampath 1 , § , Peihua Yuan 1 , § † , Isabel X. Wang 1 , # , Evelyn Prugar 1 , Fred van Leeuwen 2 and Rolf Sternglanz 1 , * 1 Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York 2 Netherlands Cancer Institute, Amsterdam, The Netherlands ABSTRACT 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Molecular and Cellular Biology American Society For Microbiology

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

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

Molecular and Cellular Biology , Volume 29 (10): 2532 – May 15, 2009

Abstract

Mutational Analysis of the Sir3 BAH Domain Reveals Multiple Points of Interaction with Nucleosomes ▿ Vinaya Sampath 1 , § , Peihua Yuan 1 , § † , Isabel X. Wang 1 , # , Evelyn Prugar 1 , Fred van Leeuwen 2 and Rolf Sternglanz 1 , * 1 Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York 2 Netherlands Cancer Institute, Amsterdam, The Netherlands ABSTRACT 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.

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Publisher
American Society For Microbiology
Copyright
Copyright © 2009 by the American society for Microbiology.
ISSN
0270-7306
eISSN
1098-5549
DOI
10.1128/MCB.01682-08
pmid
19273586
Publisher site
See Article on Publisher Site

Abstract

Mutational Analysis of the Sir3 BAH Domain Reveals Multiple Points of Interaction with Nucleosomes ▿ Vinaya Sampath 1 , § , Peihua Yuan 1 , § † , Isabel X. Wang 1 , # , Evelyn Prugar 1 , Fred van Leeuwen 2 and Rolf Sternglanz 1 , * 1 Department of Biochemistry and Cell Biology, Stony Brook University, Stony Brook, New York 2 Netherlands Cancer Institute, Amsterdam, The Netherlands ABSTRACT 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.

Journal

Molecular and Cellular BiologyAmerican Society For Microbiology

Published: May 15, 2009

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