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UPF1-like helicase grip on nucleic acids dictates processivity

Author

Listed:
  • Joanne Kanaan

    (PSL Research University)

  • Saurabh Raj

    (PSL Research University
    CNRS
    Universität Leipzig)

  • Laurence Decourty

    (Institut Pasteur)

  • Cosmin Saveanu

    (Institut Pasteur)

  • Vincent Croquette

    (PSL Research University
    CNRS)

  • Hervé Le Hir

    (PSL Research University)

Abstract

Helicases are molecular engines which translocate along nucleic acids (NA) to unwind double-strands or remodel NA–protein complexes. While they have an essential role in genome structure and expression, the rules dictating their processivity remain elusive. Here, we developed single-molecule methods to investigate helicase binding lifetime on DNA. We found that UPF1, a highly processive helicase central to nonsense-mediated mRNA decay (NMD), tightly holds onto NA, allowing long lasting action. Conversely, the structurally similar IGHMBP2 helicase has a short residence time. UPF1 mutants with variable grip on DNA show that grip tightness dictates helicase residence time and processivity. In addition, we discovered via functional studies that a decrease in UPF1 grip impairs NMD efficiency in vivo. Finally, we propose a three-state model with bound, sliding and unbound molecular clips, that can accurately predict the modulation of helicase processivity.

Suggested Citation

  • Joanne Kanaan & Saurabh Raj & Laurence Decourty & Cosmin Saveanu & Vincent Croquette & Hervé Le Hir, 2018. "UPF1-like helicase grip on nucleic acids dictates processivity," Nature Communications, Nature, vol. 9(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-06313-y
    DOI: 10.1038/s41467-018-06313-y
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