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TitleCryo-EM structures of the eukaryotic replicative helicase bound to a translocation substrate.
Journal, issue, pagesNat Commun, Vol. 7, Page 10708, Year 2016
Publish dateFeb 18, 2016
AuthorsFerdos Abid Ali / Ludovic Renault / Julian Gannon / Hailey L Gahlon / Abhay Kotecha / Jin Chuan Zhou / David Rueda / Alessandro Costa /
PubMed AbstractThe 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 ...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.
External linksNat Commun / PubMed:26888060 / PubMed Central
MethodsEM (single particle)
Resolution7.4 - 10.2 Å
Structure data

EMDB-3318:
CryoEM structure of the CMG replicative helicase bound to a DNA fork (compact state)
Method: EM (single particle) / Resolution: 7.4 Å

EMDB-3319:
CryoEM structure of the CMG replicative helicase bound to a DNA fork (relaxed state)
Method: EM (single particle) / Resolution: 9.8 Å

EMDB-3320:
CryoEM structure of the ATP-treated CMG replicative helicase (compact state)
Method: EM (single particle) / Resolution: 10.2 Å

EMDB-3321:
CryoEM structure of the ATP-treated CMG replicative helicase (relaxed state)
Method: EM (single particle) / Resolution: 9.3 Å

Source
  • Drosophila melanogaster (fruit fly)
  • synthetic construct (others)

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