Nα-acetylated Sir3 stabilizes the conformation of a nucleosome-binding loop in the BAH domain，Nature structural & Molecular Biology ，Published online: 11 August 2013

Nature structural & Molecular Biology, Published online 11 August 2013 ，doi:10.1038/nsmb.2637

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

Dongxue Yang1–3, Qianglin Fang1–3, Mingzhu Wang1,3, Ren Ren1, Hong Wang1,2, Meng He1, Youwei Sun1, Na Yang1 & Rui-Ming Xu1

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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全文链接：http://www.nature.com/nsmb/journal/vaop/ncurrent/pdf/nsmb.2637.pdf