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

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-terminal acetylated BAH domain of S.cerevisiae Sir3 bound to the nucleosome core particle revealed that the N-terminal ac...

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Detalles Bibliográficos
Autores principales: Arnaudo, Nadia, Fernández, Israel S., McLaughlin, Stephen H., Peak-Chew, Sew Y., Rhodes, Daniela, Martino, Fabrizio
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2013
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3818696/
https://www.ncbi.nlm.nih.gov/pubmed/23934150
http://dx.doi.org/10.1038/nsmb.2641
Descripción
Sumario: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-terminal acetylated BAH domain of S.cerevisiae Sir3 bound to the nucleosome core particle revealed 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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