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The centromere is an evolutionarily conserved eukaryotic protein machinery essential for precision segregation of the parental genome into two daughter cells during mitosis. Centromere protein A (CENP-A) organizes the functional centromere via a constitutive centromere-associated network composing the CENP-T complex. However, how CENP-T assembles onto the centromere remains elusive. Here we show that CENP-T binds directly to Holliday junction recognition protein (HJURP), an evolutionarily conserved chaperone involved in loading CENP-A. The binding interface of HJURP was mapped to the C terminus of CENP-T. Depletion of HJURP by CRISPR-elicited knockout minimized recruitment of CENP-T to the centromere, indicating the importance of HJURP in CEPN-T loading. Our immunofluorescence analyses indicate that HJURP recruits CENP-T to the centromere in S/G2 phase during the cell division cycle. Significantly, the HJURP binding-deficient mutant CENP-T6L failed to locate to the centromere. Importantly, CENP-T insufficiency resulted in chromosome misalignment, in particular chromosomes 15 and 18. Taken together, these data define a novel molecular mechanism underlying the assembly of CENP-T onto the centromere by a temporally regulated HJURP-CENP-T interaction. © 2019 Ding et al.


Mingrui Ding, Jiying Jiang, Fengrui Yang, Fan Zheng, Jingwen Fang, Qian Wang, Jianyu Wang, William Yao, Xu Liu, Xinjiao Gao, McKay Mullen, Ping He, Cathy Rono, Xia Ding, Jingjun Hong, Chuanhai Fu, Xing Liu, Xuebiao Yao. Holliday junction recognition protein interacts with and specifies the centromeric assembly of CENP-T. The Journal of biological chemistry. 2019 Jan 18;294(3):968-980

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PMID: 30459232

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