Cryo-EM structures of the eukaryotic replicative helicase bound to a translocation substrate View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2016-02-18

AUTHORS

Ferdos Abid Ali, Ludovic Renault, Julian Gannon, Hailey L. Gahlon, Abhay Kotecha, Jin Chuan Zhou, David Rueda, Alessandro Costa

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. More... »

PAGES

10708

References to SciGraph publications

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/ncomms10708

    DOI

    http://dx.doi.org/10.1038/ncomms10708

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1024121020

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/26888060


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