期刊
NATURE COMMUNICATIONS
卷 7, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms10708
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资金
- Francis Crick Institute - Cancer Research UK
- Francis Crick Institute - UK Medical Research Council
- Francis Crick Institute - Wellcome Trust
- Boehringer Ingelheim Fonds
- Wellcome Trust
- WT equipment grant [093305/Z/10/Z]
- Clinical Sciences Center of the Medical Research Council [RCUK MC-A658-5TY10]
- startup grant from Imperial College London
- Swiss National Science Foundation
- MRC
- BBSRC
- Wellcome Trust JIF award [060208/Z/00/Z]
- MRC [MC_UP_1102/5] Funding Source: UKRI
The Cdc45-MCM-GINS (CMG) helicase unwinds DNA during the elongation step of eukaryotic genome duplication and this process depends on the MCM ATPase function. Whether CMG translocation occurs on single- or double-stranded DNA and how ATP hydrolysis drives DNA unwinding remain open questions. Here we use cryo-electron microscopy to describe two subnanometre resolution structures of the CMG helicase trapped on a DNA fork. In the predominant state, the ring-shaped C-terminal ATPase of MCM is compact and contacts single-stranded DNA, via a set of pre-sensor 1 hairpins that spiral around the translocation substrate. In the second state, the ATPase module is relaxed and apparently substrate free, while DNA intimately contacts the downstream amino-terminal tier of the MCM motor ring. These results, supported by single-molecule FRET measurements, lead us to suggest a replication fork unwinding mechanism whereby the N-terminal and AAA+ tiers of the MCM work in concert to translocate on single-stranded DNA.
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