The N-terminal acetylation of Sir3 stabilizes its binding to the nucleosome core particle

被引：68

作者：

Arnaudo, Nadia ^{[1
]}

Fernandez, Israel S. ^{[1
]}

McLaughlin, Stephen H. ^{[1
]}

Peak-Chew, Sew Y. ^{[1
]}

Rhodes, Daniela ^{[1
]}

Martino, Fabrizio ^{[1
]}

机构：

[1] MRC, Mol Biol Lab, Struct Studies Div, Cambridge CB2 2QH, England

来源：

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

基金：

英国医学研究理事会; 瑞士国家科学基金会;

关键词：

SILENT CHROMATIN; BAH DOMAIN; SACCHAROMYCES-CEREVISIAE; ANGSTROM RESOLUTION; STRUCTURAL BASIS; AMINO-TERMINUS; YEAST; REFINEMENT;

D O I：

10.1038/nsmb.2641

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：

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.

引用

页码：1119 / +

页数：4

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