The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle.

Nat. Struct. Mol. Biol.2013 Sep;20(9):1119-21. Epub 2013 Aug 11

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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.

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The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle.

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