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dc.contributor.author
Ali, Ferdos A.
dc.contributor.author
Renault, Ludovic
dc.contributor.author
Gannon, Julian
dc.contributor.author
Gahlon, Hailey
dc.contributor.author
Kotecha, Abhay
dc.contributor.author
Zhou, Jin C.
dc.contributor.author
Rueda, David
dc.contributor.author
Costa, Alessandro
dc.date.accessioned
2020-06-17T13:33:37Z
dc.date.available
2018-12-19T16:02:22Z
dc.date.available
2018-12-21T10:59:45Z
dc.date.available
2020-06-17T13:33:37Z
dc.date.issued
2016-02-18
dc.identifier.issn
2041-1723
dc.identifier.other
10.1038/ncomms10708
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/312192
dc.identifier.doi
10.3929/ethz-b-000312192
dc.description.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.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Nature Publishing Group
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
Cryo-EM structures of the eukaryotic replicative helicase bound to a translocation substrate
en_US
dc.type
Journal Article
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
dc.date.published
2016-02-18
ethz.journal.title
Nature Communications
ethz.journal.volume
7
en_US
ethz.journal.abbreviated
Nat Commun
ethz.pages.start
10708
en_US
ethz.size
11 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.publication.place
London
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02070 - Dep. Gesundheitswiss. und Technologie / Dep. of Health Sciences and Technology::02701 - Inst.f. Lebensmittelwiss.,Ernährung,Ges. / Institute of Food, Nutrition, and Health::03853 - Sturla, Shana / Sturla, Shana
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02070 - Dep. Gesundheitswiss. und Technologie / Dep. of Health Sciences and Technology::02701 - Inst.f. Lebensmittelwiss.,Ernährung,Ges. / Institute of Food, Nutrition, and Health::03853 - Sturla, Shana / Sturla, Shana
ethz.identifier.orcidWorkCode
25107090
ethz.date.deposited
2018-12-19T16:02:34Z
ethz.source
FORM
ethz.eth
no
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2018-12-21T10:59:49Z
ethz.rosetta.lastUpdated
2021-02-15T14:44:35Z
ethz.rosetta.exportRequired
true
ethz.rosetta.versionExported
true
ethz.COinS
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