@article{Ali:2016:10.1038/ncomms10708,
author = {Ali, FA and Renault, L and Gannon, J and Gahlon, HL and Kotecha, A and Zhou, JC and Rueda, D and Costa, A},
doi = {10.1038/ncomms10708},
journal = {Nature Communications},
title = {Cryo-EM structures of the eukaryotic replicative helicase bound to a translocation substrate},
url = {http://dx.doi.org/10.1038/ncomms10708},
volume = {7},
year = {2016}
}

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TY  - JOUR
AB  - 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.
AU  - Ali,FA
AU  - Renault,L
AU  - Gannon,J
AU  - Gahlon,HL
AU  - Kotecha,A
AU  - Zhou,JC
AU  - Rueda,D
AU  - Costa,A
DO  - 10.1038/ncomms10708
PY  - 2016///
SN  - 2041-1723
TI  - Cryo-EM structures of the eukaryotic replicative helicase bound to a translocation substrate
T2  - Nature Communications
UR  - http://dx.doi.org/10.1038/ncomms10708
UR  - http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000371035200009&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=1ba7043ffcc86c417c072aa74d649202
UR  - http://hdl.handle.net/10044/1/30759
VL  - 7
ER  - 

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