Ontology highlight
ABSTRACT:
SUBMITTER: Arnaudo N
PROVIDER: S-EPMC3818696 | biostudies-literature | 2013 Sep
REPOSITORIES: biostudies-literature
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]