Abstract
The N-terminal acetylation of Sir3 is essential for heterochromatin establishment and maintenance in yeast, but its mechanism of action is unknown. The crystal structure of the N-terminally acetylated BAH domain of Saccharomyces cerevisiae Sir3 bound to the nucleosome core particle reveals that the N-terminal acetylation stabilizes the interaction of Sir3 with the nucleosome. Additionally, we present a new method for the production of protein-nucleosome complexes for structural analysis.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Acetylation
-
Crystallography, X-Ray
-
Macromolecular Substances / chemistry
-
Macromolecular Substances / isolation & purification
-
Models, Molecular
-
Mutagenesis, Site-Directed
-
Nucleosomes / metabolism*
-
Protein Conformation
-
Protein Interaction Domains and Motifs
-
Protein Stability
-
Recombinant Proteins / chemistry
-
Recombinant Proteins / genetics
-
Recombinant Proteins / metabolism
-
Saccharomyces cerevisiae / genetics
-
Saccharomyces cerevisiae / metabolism
-
Silent Information Regulator Proteins, Saccharomyces cerevisiae / chemistry*
-
Silent Information Regulator Proteins, Saccharomyces cerevisiae / genetics
-
Silent Information Regulator Proteins, Saccharomyces cerevisiae / metabolism*
-
Static Electricity
Substances
-
Macromolecular Substances
-
Nucleosomes
-
Recombinant Proteins
-
SIR3 protein, S cerevisiae
-
Silent Information Regulator Proteins, Saccharomyces cerevisiae