The novel interaction mode among centromere sub-complex CENP-O/P/U/Q/R
The novel interaction mode among centromere sub-complex CENP-O/P/U/Q/R
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DOI：
10.1002/jmr.2892
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发表时间：
2021-03-03
影响因子：
2.7
通讯作者：
He, Xiaojing
中科院分区：
文献类型：
--
作者：
Cao, Beibei;Zhao, Congcong;He, Xiaojing
在真核细胞中，着丝点对姐妹染色体的精确分离至关重要。在着丝点亚基中，五种蛋白质CENP-O/P/U/Q/R形成一个稳定的复合物，称为CENP-O类，是着丝点正常功能所必需的。虽然酵母昏迷复合体（CENP-O/P/U/Q同源物）的功能和结构已经被广泛揭示，但人类CENP-O类之间的组装机制和细节相互作用仍存在很大差异。在这里，我们发现了CENP-U的片段（残基241-360）和CENP-Q的c端一半是形成杂络合物并在体外与CENP-O/P亚络合物相互作用所必需的。我们首次在体外证明了CENP-R不直接与CENP-O/P相互作用，但确实与CENP-U和CENP-Q相互作用。此外，CENP-R的N端和c端都需要与CENP-U和CENP-Q相互作用。我们的研究确定了一种新的相互作用模式，可能有助于揭示脊椎动物CENP-O类的组装机制。
The kinetochore is essential for the accurate segregation of sister chromosome in the eukaryote cell. Among the kinetochore subunits, five proteins CENP-O/P/U/Q/R form a stable complex, referred to as CENP-O class, and are required for proper kinetochore function. Although the function and structure of yeast COMA complex (CENP-O/P/U/Q homologs) have been revealed extensively, the assembly mechanism and detail interactions among human CENP-O class are significantly different and remain largely unclear. Here, we identified the fragment (residues 241-360) of CENP-U and the C-terminal half of CENP-Q are essential to form a hetero-complex and interact with CENP-O/P sub-complex in vitro. We for the first time showed that CENP-R does not directly interact with CENP-O/P in vitro, but indeed interact with CENP-U and CENP-Q. Furthermore, both the N- and C-terminus of CENP-R are required for the interaction with CENP-U and CENP-Q. Our research pinpointed a novel interaction pattern that might shed light on the assembly mechanism of vertebrate CENP-O class.