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. 2013 Sep;20(9):1116-8.
doi: 10.1038/nsmb.2637. Epub 2013 Aug 11.

Nα-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain

Dongxue Yang  1 , Qianglin Fang, Mingzhu Wang, Ren Ren, Hong Wang, Meng He, Youwei Sun, Na Yang, Rui-Ming Xu
Affiliations

Nα-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain

Dongxue Yang et al. Nat Struct Mol Biol. 2013 Sep.

Abstract

In Saccharomyces cerevisiae, acetylation of the Sir3 N terminus is important for transcriptional silencing. This covalent modification promotes the binding of the Sir3 BAH domain to the nucleosome, but a mechanistic understanding of this phenomenon is lacking. By X-ray crystallography, we show here that the acetylated N terminus of Sir3 does not interact with the nucleosome directly. Instead, it stabilizes a nucleosome-binding loop in the BAH domain.

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