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

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

doi:10.1038/ncomms10708

Nature Communications (Feb 2016)

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

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

Affiliations

Ferdos Abid Ali: Macromolecular Machines, Clare Hall Laboratory, The Francis Crick Institute, Blanche Lane, South Mimms EN6 3LD, UK
Ludovic Renault: Macromolecular Machines, Clare Hall Laboratory, The Francis Crick Institute, Blanche Lane, South Mimms EN6 3LD, UK
Julian Gannon: Macromolecular Machines, Clare Hall Laboratory, The Francis Crick Institute, Blanche Lane, South Mimms EN6 3LD, UK
Hailey L. Gahlon: Department of Medicine, Section of Virology and Single Molecule Imaging Group, MRC Clinical Centre, Imperial College London
Abhay Kotecha: Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, UK
Jin Chuan Zhou: Macromolecular Machines, Clare Hall Laboratory, The Francis Crick Institute, Blanche Lane, South Mimms EN6 3LD, UK
David Rueda: Department of Medicine, Section of Virology and Single Molecule Imaging Group, MRC Clinical Centre, Imperial College London
Alessandro Costa: Macromolecular Machines, Clare Hall Laboratory, The Francis Crick Institute, Blanche Lane, South Mimms EN6 3LD, UK

DOI: https://doi.org/10.1038/ncomms10708
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 11

Abstract

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The Cdc45-MCM-GINS (CMG) helicase unwinds DNA during replication, a process that requires the ATPase-dependent activity of the MCM complex. Using cryo-EM reconstructions of the CMG complex in different conformations, the authors propose a model where the N-terminal and AAA+ domains of MCM work in concert to translocate along DNA.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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