Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2
2017-06-02
发表期刊NUCLEIC ACIDS RESEARCH (IF:16.6[JCR-2023],16.1[5-Year])
ISSN0305-1048
卷号45期号:10页码:5707-5719
发表状态已发表
DOI10.1093/nar/gkx142
摘要HBO1, a member of the MYST family of histone acetyltransferases (HATs), is required for global acetylation of histone H3K14 and embryonic development. It functions as a catalytic subunit in multisubunit complexes comprising a BRPF1/2/3 or JADE1/2/3 scaffold protein, and two accessory proteins. BRPF2 has been shown to be important for the HAT activity of HBO1 toward H3K14. Here we demonstrated that BRPF2 can regulate the HAT activity of HBO1 toward free H3 and H4, and nucleosomal H3. Particularly, a short N-terminal region of BRPF2 is sufficient for binding to HBO1 and can potentiate its activity toward H3K14. The crystal structure of the HBO1 MYST domain in complex with this segment of BRPF2 together with the biochemical and cell biological data revealed the key residues responsible for the HBO1-BRPF2 interaction. Our structural and functional data together indicate that the N-terminal region of BRPF2 plays an important role in the binding of HBO1 and a minor role in the binding of nucleosomes, which provide new mechanistic insights into the regulation of the HAT activity of HBO1 by BRPF2.
收录类别SCI
语种英语
资助项目Ministry of Science and Technology of China[2013CB910404]
WOS研究方向Biochemistry & Molecular Biology
WOS类目Biochemistry & Molecular Biology
WOS记录号WOS:000402510700024
出版者OXFORD UNIV PRESS
WOS关键词PHD FINGER ; H3 TAIL ; MOLECULAR-BASIS ; HAT COMPLEXES ; ACETYLATION ; CHROMATIN ; RECOGNITION ; DOMAIN ; NUA4 ; DNA
原始文献类型Article
通讯作者Ding, Jianping
引用统计
正在获取...
文献类型期刊论文
条目标识符https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/1340
专题生命科学与技术学院_特聘教授组_丁建平组
通讯作者Ding, Jianping
作者单位
1.Chinese Acad Sci, Ctr Excellence Mol Cell Sci, Natl Ctr Prot Sci Shanghai, Shanghai Inst Biochem & Cell Biol,State Key Lab M, 320 Yue Yang Rd, Shanghai 200031, Peoples R China
2.Univ Chinese Acad Sci, Chinese Acad Sci, 320 Yue Yang Rd, Shanghai 200031, Peoples R China
3.Shanghai Tech Univ, Sch Life Sci & Technol, 100 Haike Rd, Shanghai 201210, Peoples R China
4.Chinese Acad Sci, Shanghai Sci Res Ctr, 333 Haike Rd, Shanghai 201210, Peoples R China
5.Fudan Univ, Collaborat Innovat Ctr Genet & Dev, 2005 Songhu Rd, Shanghai 200438, Peoples R China
通讯作者单位生命科学与技术学院
推荐引用方式
GB/T 7714
Tao, Ye,Zhong, Chen,Zhu, Junjun,et al. Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2[J]. NUCLEIC ACIDS RESEARCH,2017,45(10):5707-5719.
APA Tao, Ye,Zhong, Chen,Zhu, Junjun,Xu, Shutong,&Ding, Jianping.(2017).Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2.NUCLEIC ACIDS RESEARCH,45(10),5707-5719.
MLA Tao, Ye,et al."Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2".NUCLEIC ACIDS RESEARCH 45.10(2017):5707-5719.
条目包含的文件
文件名称/大小 文献类型 版本类型 开放类型 使用许可
个性服务
查看访问统计
谷歌学术
谷歌学术中相似的文章
[Tao, Ye]的文章
[Zhong, Chen]的文章
[Zhu, Junjun]的文章
百度学术
百度学术中相似的文章
[Tao, Ye]的文章
[Zhong, Chen]的文章
[Zhu, Junjun]的文章
必应学术
必应学术中相似的文章
[Tao, Ye]的文章
[Zhong, Chen]的文章
[Zhu, Junjun]的文章
相关权益政策
暂无数据
收藏/分享
文件名: 1340.pdf
格式: Adobe PDF
此文件暂不支持浏览
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。