期刊
ISCIENCE
卷 25, 期 9, 页码 -出版社
CELL PRESS
DOI: 10.1016/j.isci.2022.104976
关键词
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资金
- National Natural Science Foundation of China [32071188, 31925023, 21827810]
- Hong Kong Special Administrative Region [GRF16103719, GRF16101120, GRF16101121, SZSTI19SC02, SMSEGL20SC01-H, AoE/M-403-16, AoE/M-401/20, VPRDO19RD03-6]
- Ministry of Science and Technology of the People's Republic of China [2021YFA1300204]
- Beijing Frontier Research Center for Biological Structure
- Bejing Advanced Innovation Center for Structure Biology
- Guangdong Basic and Applied Basic Research Foundation [2020A1515010034, 2021A1515220104]
This study presents the cryo-EM structure of human MCM2-7 complex, revealing its capability to self-assemble into a loose double hexamer and suggesting a novel loading mechanism. The high-resolution cryo-EM structure of human MCM2-7 is critical for understanding the molecular mechanisms governing human DNA replication.
The central step in the initiation of eukaryotic DNA replication is the loading of the minichromosome maintenance 2-7 (MCM2-7) complex, the core of the replicative DNA helicase, onto chromatin at replication origin. Here, we reported the cryo-EM structure of endogenous human single hexameric MCM2-7 complex with a resolution at 4.4 angstrom, typically an open-ring hexamer with a gap between Mcm2 and Mcm5. Strikingly, further analysis revealed that human MCM2-7 can self-associate to form a loose double hexamer which potentially implies a novel mechanism underlying the MCM2-7 loading in eukaryote. The high-resolution cryo-EM structure of human MCM2-7 is critical for understanding the molecular mechanisms governing human DNA replication, especially the MCM2-7 chromatin loading and pre-replicative complex assembly.
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