Faithful inheritance of genetic information requires precise segregation of sister chromatids during mitosis, which entails the attachment of spindle microtubules to each chromatid at a specialized locus, known as the centromere. 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). A recent study solved the crystal structure of an HJURP–CENP-A–histone H4 complex and showed that HJURP binds a CENP-A–H4 heterodimer. This study was led by Professor Ruiming Xu from the Institute of Biophysics, Chinese Academy of Sciences (IBP CAS). Xu’s group found that the C-terminal b-sheet domain of HJURP caps the DNA-binding region of the histone heterodimer, preventing it from spontaneous association with DNA. They also discovered 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.

This work was published on May 1st in the latest issue of Genes & Development. Just four days after the on line publication, Dr Yamini Dalal from National Cancer Institute (NIH, USA) highly recommended this work for its good quality through Faculty of 1000. He pointed out that the research uncovered a key residue allows HJURP to specifically recognize CENP-A and its results will undoubtedly be the focus of future studies. The F1000 Article Factor of this paper is 10 which means exceptional.

This work was conducted in collaborating with Dr Guohong Li’s group from IBP CAS and Drs Xuebiao Yao and Yunyu Shi’s groups from University of Science and Technology of China. It was supported by grants from the Ministry of Science and Technology of China, the National Natural Science Foundation of China and CAS.