网站地图 联系我们搜索内部网English | 中国科学院
首页 所况简介 机构设置 科研队伍 科学研究平台 院地合作 党群园地 国际交流 博士后 研究生教育 科学传播 信息公开
科研进展
成果报道
最新重要论文(影响因子PNAS及以上)
发表论文数据库
所级学术报告
科学成果
发表论文
专著
专利
获奖
专题
所史丛书
所庆专辑
建所50周年画册
现在位置:首页 > 科研进展 > 最新重要论文(影响因子PNAS及以上)
Multisite Substrate Recognition in Asf1-Dependent Acetylation of Histone H3 K56 by Rtt109, Cell, 9 August 2018
2018-08-10 | 【     】【打印】【关闭

Cell, 9 August 2018,DOI: https://doi.org/10.1016/j.cell.2018.07.005

Multisite Substrate Recognition in Asf1-Dependent Acetylation of Histone H3 K56 by Rtt109

Lin Zhang,Albert Serra-Cardona,Hui Zhou,Mingzhu Wang,Na Yang,Zhiguo Zhang,Rui-Ming Xu

Abstract

Rtt109 is a unique histone acetyltransferase acetylating histone H3 lysine 56 (H3K56), a modification critical for DNA replication-coupled nucleosome assembly and genome stability. In cells, histone chaperone Asf1 is essential for H3K56 acetylation, yet the mechanisms for H3K56 specificity and Asf1 requirement remain unknown. We have determined the crystal structure of the Rtt109-Asf1-H3-H4 complex and found that unwinding of histone H3 αN, where K56 is normally located, and stabilization of the very C-terminal β strand of histone H4 by Asf1 are prerequisites for H3K56 acetylation. Unexpectedly, an interaction between Rtt109 and the central helix of histone H3 is also required. The observed multiprotein, multisite substrate recognition mechanism among histone modification enzymes provides mechanistic understandings of Rtt109 and Asf1 in H3K56 acetylation, as well as valuable insights into substrate recognition by histone modification enzymes in general.

文章链接:https://www.cell.com/cell/fulltext/S0092-8674(18)30899-7

相关报道:http://www.ibp.cas.cn/kyjz/zxdt/201808/t20180810_5054488.html

 

评 论
                 
版权所有:中国科学院生物物理研究所     京ICP备05002792号 京公网安备 110402500011 号
地址:北京市朝阳区大屯路15号(100101) 电话:010-64889872
意见反馈联系人:马秋云 电子邮件:maqiuyun@moon.ibp.ac.cn