2011年5月，我室生物大分子结构与功能研究部姚雪彪施蕴渝教授研究组与中科院合作在GENES & DEVELOPMENT上发表题为Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP的论文。

Source: GENES & DEVELOPMENT Volume: 25 Issue: 9 Pages: 901-906 Published: MAY 1 2011
Hu H (Hu, Hao)1,2, Liu Y (Liu, Yang)1, Wang MZ (Wang, Mingzhu)1, Fang JN (Fang, Junnan)1,2, Huang HD (Huang, Hongda)3,4, Yang N (Yang, Na)1, Li YB (Li, Yanbo)1, Wang JY (Wang, Jianyu)3,4, Yao XB (Yao, Xuebiao)3,4, Shi YY (Shi, Yunyu)3,4, Li GH (Li, Guohong)1, Xu RM (Xu, Rui-Ming)1
Addresses:
1. Chinese Acad Sci, Natl Lab Biomacromol, Inst Biophys, Beijing 100101, Peoples R China
2. Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China
3. Univ Sci & Technol China, Hefei Natl Lab Phys Sci Microscale, Hefei 230026, Anhui Peoples R China
4. Univ Sci & Technol China, Sch Life Sci, Hefei 230026, Anhui Peoples R China
E-mail Addresses: rmxu@sun5.ibp.ac.cn

Reprint Address: Xu, RM (reprint author), Chinese Acad Sci, Natl Lab Biomacromol, Inst Biophys, Beijing 100101, Peoples R China

Abstract: In higher eukaryotes, the centromere is epigenetically specified by the histone H3 variant Centromere Protein-A (CENP-A). Deposition of CENP-A to the centromere requires histone chaperone HJURP (Holliday junction recognition protein). The crystal structure of an HJURP-CENP-A-histone H4 complex shows that HJURP binds a CENP-A-H4 heterodimer. The C-terminal beta-sheet domain of HJURP caps the DNA-binding region of the histone heterodimer, preventing it from spontaneous association with DNA. Our analysis also revealed a novel site in CENP-A that distinguishes it from histone H3 in its ability to bind HJURP. These findings provide key information for specific recognition of CENP-A and mechanistic insights into the process of centromeric chromatin assembly.