Molecular Basis for ATP-Hydrolysis-Driven DNA Translocation by the CMG Helicase of the Eukaryotic Replisome

Patrik Eickhoff, Hazal B. Kose, Fabrizio Martino, Tatjana Petojevic, Ferdos Abid Ali, Julia Locke, Nele Tamberg, Andrea Nans, James M. Berger, Michael R. Botchan, Hasan Yardimci, Alessandro Costa

Research output: Contribution to journalArticle

Abstract

Eickhoff et al. used cryo-EM to image DNA unwinding by the eukaryotic replicative helicase, Cdc45-MCM-GINS. As the hexameric MCM ring hydrolyses ATP, DNA is spooled asymmetrically around the ring pore. This asymmetry explains why selected ATPase sites are essential for DNA translocation. Understanding DNA unwinding informs on replication fork progression.

Original languageEnglish (US)
Pages (from-to)2673-2688.e8
JournalCell Reports
Volume28
Issue number10
DOIs
StatePublished - Sep 3 2019

Keywords

  • AAA+ ATPase
  • DNA replication
  • DNA unwinding
  • cryo-EM
  • helicase
  • molecular motor

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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  • Cite this

    Eickhoff, P., Kose, H. B., Martino, F., Petojevic, T., Abid Ali, F., Locke, J., Tamberg, N., Nans, A., Berger, J. M., Botchan, M. R., Yardimci, H., & Costa, A. (2019). Molecular Basis for ATP-Hydrolysis-Driven DNA Translocation by the CMG Helicase of the Eukaryotic Replisome. Cell Reports, 28(10), 2673-2688.e8. https://doi.org/10.1016/j.celrep.2019.07.104