Abstract
In Saccharomyces cerevisiae, acetylation of the Sir3 N terminus is important for transcriptional silencing. This covalent modification promotes the binding of the Sir3 BAH domain to the nucleosome, but a mechanistic understanding of this phenomenon is lacking. By X-ray crystallography, we show here that the acetylated N terminus of Sir3 does not interact with the nucleosome directly. Instead, it stabilizes a nucleosome-binding loop in the BAH domain.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetylation
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Amino Acid Sequence
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Crystallography, X-Ray
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Gene Silencing
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Models, Molecular
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Nucleosomes / metabolism*
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Protein Conformation
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Protein Interaction Domains and Motifs
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Protein Stability
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism
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Silent Information Regulator Proteins, Saccharomyces cerevisiae / chemistry*
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Silent Information Regulator Proteins, Saccharomyces cerevisiae / genetics
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Silent Information Regulator Proteins, Saccharomyces cerevisiae / metabolism*
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Static Electricity
Substances
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Nucleosomes
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Recombinant Proteins
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SIR3 protein, S cerevisiae
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Silent Information Regulator Proteins, Saccharomyces cerevisiae
Associated data
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PDB/4KUD
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PDB/4KUI
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PDB/4KUL