Abstract:
: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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Abid Ali F,Renault L,Gannon J,Gahlon HL,Kotecha A,Zhou JC,Rueda D,Costa Adoi
10.1038/ncomms10708subject
Has Abstractpub_date
2016-02-18 00:00:00pages
10708issn
2041-1723pii
ncomms10708journal_volume
7pub_type
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