TY - JOUR
T1 - Mitotic regulator Mis18β interacts with and specifies the centromeric assembly of molecular chaperone holliday junction recognition protein (HJURP)
AU - Wang, Jianyu
AU - Liu, Xing
AU - Dou, Zhen
AU - Chen, Liang
AU - Jiang, Hao
AU - Fu, Chuanhai
AU - Fu, Guosheng
AU - Liu, Dan
AU - Zhang, Jiancun
AU - Zhu, Tongge
AU - Fang, Jingwen
AU - Zang, Jianye
AU - Cheng, Jinke
AU - Teng, Maikun
AU - Ding, Xia
AU - Yao, Xuebiao
PY - 2014/3/21
Y1 - 2014/3/21
N2 - The centromere is essential for precise and equal segregation of the parental genome into two daughter cells during mitosis. CENP-A is a unique histone H3 variant conserved in eukaryotic centromeres. The assembly of CENP-A to the centromere is mediated by Holliday junction recognition protein (HJURP) in early G1 phase. However, it remains elusive how HJURP governs CENP-A incorporation into the centromere. Here we show that human HJURP directly binds to Mis18β, a component of the Mis18 complex conserved in the eukaryotic kingdom. A minimal region of HJURP for Mis18β binding was mapped to residues 437-460. Depletion of Mis18β by RNA interference dramatically impaired HJURP recruitment to the centromere, indicating the importance of Mis18β in HJURP loading. Interestingly, phosphorylation of HJURP by CDK1 weakens its interaction with Mis18β, consistent with the notion that assembly of CENP-A to the centromere is achieved after mitosis. Taken together, these data define a novel molecular mechanism underlying the temporal regulation of CENP-A incorporation into the centromere by accurate Mis18β-HJURP interaction.
AB - The centromere is essential for precise and equal segregation of the parental genome into two daughter cells during mitosis. CENP-A is a unique histone H3 variant conserved in eukaryotic centromeres. The assembly of CENP-A to the centromere is mediated by Holliday junction recognition protein (HJURP) in early G1 phase. However, it remains elusive how HJURP governs CENP-A incorporation into the centromere. Here we show that human HJURP directly binds to Mis18β, a component of the Mis18 complex conserved in the eukaryotic kingdom. A minimal region of HJURP for Mis18β binding was mapped to residues 437-460. Depletion of Mis18β by RNA interference dramatically impaired HJURP recruitment to the centromere, indicating the importance of Mis18β in HJURP loading. Interestingly, phosphorylation of HJURP by CDK1 weakens its interaction with Mis18β, consistent with the notion that assembly of CENP-A to the centromere is achieved after mitosis. Taken together, these data define a novel molecular mechanism underlying the temporal regulation of CENP-A incorporation into the centromere by accurate Mis18β-HJURP interaction.
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U2 - 10.1074/jbc.M113.529958
DO - 10.1074/jbc.M113.529958
M3 - Article
C2 - 24519934
AN - SCOPUS:84896916856
SN - 0021-9258
VL - 289
SP - 8326
EP - 8336
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 12
ER -