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

被引：56

作者：

Yang, Dongxue ^{[1
,2
]}

Fang, Qianglin ^{[1
,2
]}

Wang, Mingzhu ^{[1
]}

Ren, Ren ^{[1
]}

Wang, Hong ^{[1
,2
]}

He, Meng ^{[1
]}

Sun, Youwei ^{[1
]}

Yang, Na ^{[1
]}

Xu, Rui-Ming ^{[1
]}

机构：

[1] Chinese Acad Sci, Inst Biophys, Natl Lab Biomacromol, Beijing 100080, Peoples R China

[2] Univ Chinese Acad Sci, Beijing, Peoples R China

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2013年 / 20卷 / 09期

关键词：

STRUCTURAL BASIS; SACCHAROMYCES-CEREVISIAE; RECOGNITION COMPLEX; SILENCED CHROMATIN; YEAST; CONSERVATION; TERMINUS; ORC1P;

D O I：

10.1038/nsmb.2637

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：1116 / +

页数：4

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