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Reference: Arnaudo N, et al. (2013) The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle. Nat Struct Mol Biol 20(9):1119-21

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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.

Reference Type
Journal Article
Authors
Arnaudo N, Fernandez IS, McLaughlin SH, Peak-Chew SY, Rhodes D, Martino F
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