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RecG and UvsW catalyse robust DNA rewinding critical for stalled DNA replication fork rescue

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  • Maria Manosas

    (Departament de Física Fonamental, Facultat de Física, Universitat de Barcelona
    CIBER-BBN de Bioingenieria, Biomateriales y Nanomedicina, Instituto de Sanidad Carlos III)

  • Senthil K. Perumal

    (The Pennsylvania State University)

  • Piero R. Bianco

    (Center for Single Molecule Biophysics, University at Buffalo)

  • Felix Ritort

    (Departament de Física Fonamental, Facultat de Física, Universitat de Barcelona
    CIBER-BBN de Bioingenieria, Biomateriales y Nanomedicina, Instituto de Sanidad Carlos III)

  • Stephen J. Benkovic

    (The Pennsylvania State University)

  • Vincent Croquette

    (Laboratoire de Physique Statistique, Ecole Normale Supérieure, UPMC Univ. Paris 06, Université Paris Diderot, CNRS
    Ecole Normale Supérieure)

Abstract

Helicases that both unwind and rewind DNA have central roles in DNA repair and genetic recombination. In contrast to unwinding, DNA rewinding by helicases has proved difficult to characterize biochemically because of its thermodynamically downhill nature. Here we use single-molecule assays to mechanically destabilize a DNA molecule and follow, in real time, unwinding and rewinding by two DNA repair helicases, bacteriophage T4 UvsW and Escherichia coli RecG. We find that both enzymes are robust rewinding enzymes, which can work against opposing forces as large as 35 pN, revealing their active character. The generation of work during the rewinding reaction allows them to couple rewinding to DNA unwinding and/or protein displacement reactions central to the rescue of stalled DNA replication forks. The overall results support a general mechanism for monomeric rewinding enzymes.

Suggested Citation

  • Maria Manosas & Senthil K. Perumal & Piero R. Bianco & Felix Ritort & Stephen J. Benkovic & Vincent Croquette, 2013. "RecG and UvsW catalyse robust DNA rewinding critical for stalled DNA replication fork rescue," Nature Communications, Nature, vol. 4(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3368
    DOI: 10.1038/ncomms3368
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