A Ctf4 trimer couples the CMG helicase to DNA polymerase α in the eukaryotic replisome

Aline C. Simon, Jin C. Zhou, Rajika L. Perera, Frederick van Deursen, Cecile Evrin, Marina E. Ivanova, Mairi L. Kilkenny, Ludovic Renault, Svend Kjaer, Dijana Matak-Vinković, Karim Labib, Alessandro Costa () and Luca Pellegrini ()
Additional contact information
Aline C. Simon: University of Cambridge, Cambridge CB2 1GA, UK
Jin C. Zhou: Clare Hall Laboratories, Cancer Research UK London Research Institute, London EN6 3LD, UK
Rajika L. Perera: University of Cambridge, Cambridge CB2 1GA, UK
Frederick van Deursen: Cancer Research UK Manchester Institute, University of Manchester, Manchester M20 4BX, UK
Cecile Evrin: MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK
Marina E. Ivanova: University of Cambridge, Cambridge CB2 1GA, UK
Mairi L. Kilkenny: University of Cambridge, Cambridge CB2 1GA, UK
Ludovic Renault: Clare Hall Laboratories, Cancer Research UK London Research Institute, London EN6 3LD, UK
Svend Kjaer: Protein purification, Cancer Research UK London Research Institute, London WC2A 3LY, UK
Dijana Matak-Vinković: University of Cambridge, Cambridge CB2 1EW, UK
Karim Labib: MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK
Alessandro Costa: Clare Hall Laboratories, Cancer Research UK London Research Institute, London EN6 3LD, UK
Luca Pellegrini: University of Cambridge, Cambridge CB2 1GA, UK

Nature, 2014, vol. 510, issue 7504, 293-297

Abstract: This study shows how the yeast Ctf4 protein couples the DNA helicase, Cdc45–MCM–GINS, to DNA polymerase α — the GINS subunit of the helicase and the polymerase use a similar interaction to bind Ctf4, suggesting that, as Ctf4 is a trimer, two polymerases could be simultaneously coupled to a single helicase during lagging-strand synthesis.

Date: 2014
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DOI: 10.1038/nature13234

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