Structure insights into the molecular mechanism of the interaction between UHRF2 and PCNA

被引:9
作者
Chen, Wanbiao [1 ,2 ]
Wu, Minhao [1 ,2 ]
Hang, Tianrong [1 ,2 ]
Wang, Chengliang [1 ,2 ]
Zhang, Xuan [1 ,2 ]
Zang, Jianye [1 ,2 ]
机构
[1] Univ Sci & Technol China, Hefei Natl Lab Phys Sci Microscale, Sch Life Sci, Collaborat Innovat Ctr Chem Life Sci,CAS Ctr Exce, 96 Jinzhai Rd, Hefei 230026, Anhui, Peoples R China
[2] Chinese Acad Sci, Key Lab Struct Biol, Hefei 230026, Anhui, Peoples R China
基金
中国国家自然科学基金;
关键词
UHRF2; PIP-box; PCNA; Structure; Molecular mechanism; CELL-CYCLE NETWORK; CRYSTAL-STRUCTURE; UBIQUITIN LIGASE; NIRF; BINDING;
D O I
10.1016/j.bbrc.2017.09.102
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
UHRF2 (Ubiquitin-like with PHD and ring finger domains 2) is an E3 ubiquitin ligase that plays important roles in DNA methylation, histone modifications and cell cycle regulation by interacting with multiple epigenetic or cell-cycle related proteins. Previous studied have identified PCNA (Proliferating cell nuclear antigen) as an interacting partner of UHRF2 by using the antibody microarray. However, the molecular mechanism and the function of UHRF2-PCNA interaction remains unclear. Here, we report the complex structure of PCNA and the peptide ((784)NEILQTLLDLFFPGYSK(800)) derived from UHRF2 that contains a PIP box. Structural analysis combined with mutagenesis experiments provide the molecular basis for the recognition of UHRF2 by PCNA via PIP-box. (C) 2017 Elsevier Inc. All rights reserved.
引用
收藏
页码:575 / 580
页数:6
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