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Fork sensing and strand switching control antagonistic activities of RecQ helicases

Author

Listed:
  • Daniel Klaue

    (Biotechnology Center, Technische Universität Dresden)

  • Daniela Kobbe

    (Botanical Institute II, Karlsruhe Institute of Technology (KIT))

  • Felix Kemmerich

    (Biotechnology Center, Technische Universität Dresden)

  • Alicja Kozikowska

    (Biotechnology Center, Technische Universität Dresden)

  • Holger Puchta

    (Botanical Institute II, Karlsruhe Institute of Technology (KIT))

  • Ralf Seidel

    (Biotechnology Center, Technische Universität Dresden
    Institute of Molecular Cell Biology, University of Münster, Münster)

Abstract

RecQ helicases have essential roles in maintaining genome stability during replication and in controlling double-strand break repair by homologous recombination. Little is known about how the different RecQ helicases found in higher eukaryotes achieve their specialized and partially opposing functions. Here, we investigate the DNA unwinding of RecQ helicases from Arabidopsis thaliana, AtRECQ2 and AtRECQ3 at the single-molecule level using magnetic tweezers. Although AtRECQ2 predominantly unwinds forked DNA substrates in a highly repetitive fashion, AtRECQ3 prefers to rewind, that is, to close preopened DNA forks. For both enzymes, this process is controlled by frequent strand switches and active sensing of the unwinding fork. The relative extent of the strand switches towards unwinding or towards rewinding determines the predominant direction of the enzyme. Our results provide a simple explanation for how different biological activities can be achieved by rather similar members of the RecQ family.

Suggested Citation

  • Daniel Klaue & Daniela Kobbe & Felix Kemmerich & Alicja Kozikowska & Holger Puchta & Ralf Seidel, 2013. "Fork sensing and strand switching control antagonistic activities of RecQ helicases," Nature Communications, Nature, vol. 4(1), pages 1-9, October.
    • Handle: RePEc:nat:natcom:v:4:y:2013:i:1:d:10.1038_ncomms3024
    DOI: 10.1038/ncomms3024
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