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

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.

SUBMITTER: Arnaudo N

PROVIDER: S-EPMC3818696 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature

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

Arnaudo Nadia N Fernández Israel S IS McLaughlin Stephen H SH Peak-Chew Sew Y SY Rhodes Daniela D Martino Fabrizio F

Nature structural & molecular biology 20130811 9

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. ...[more]

PMID: 23934150

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