The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle
Fernández, Israel S.
McLaughlin, Stephen H.
Peak-Chew, Sew Y.
Date of Issue2013
School of Biological Sciences
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.
DRNTU::Science::Biological sciences::Molecular biology
Nature structural & molecular biology