Structure of a CENP-A–histone H4 heterodimer in complex with chaperone HJURP
- Hao Hu1,2,
- Yang Liu1,
- Mingzhu Wang1,
- Junnan Fang1,2,
- Hongda Huang3,
- Na Yang1,
- Yanbo Li1,
- Jianyu Wang3,
- Xuebiao Yao3,
- Yunyu Shi3,
- Guohong Li1 and
- Rui-Ming Xu1,4
- 1National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China;
- 2Graduate University of Chinese Academy of Sciences, Beijing 100049, China;
- 3Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, 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 β-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.
Keywords
Footnotes
-
↵4 Corresponding author.
E-MAIL rmxu{at}sun5.ibp.ac.cn; FAX 86-10-648888023.
-
Article published online ahead of print. Article and publication date are online at http://www.genesdev.org/cgi/doi/10.1101/gad.2045111.
-
Supplemental material is available for this article.
- Received February 24, 2011.
- Accepted March 14, 2011.
- Copyright © 2011 by Cold Spring Harbor Laboratory Press
