Journal
NATURE COMMUNICATIONS
Volume 9, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-018-06313-y
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Funding
- ANR CLEANMD from the French Agence Nationale de la Recherche [ANR-14-CE10-0014]
- program Investissements d'Avenir [ANR-10-LABX-54 MEMOLIFE, ANR-10-IDEX-0001-02 PSL*]
- European Research Council grant Magreps [267862]
- Fondation ARC pour la recherche sur le cancer PhD fellowship
- Centre National de Recherche Scientifique
- Ecole Normale Superieure
- Institut National de la Sante et de la Recherche Medicale, France
- European Research Council (ERC) [267862] Funding Source: European Research Council (ERC)
- Agence Nationale de la Recherche (ANR) [ANR-14-CE10-0014] Funding Source: Agence Nationale de la Recherche (ANR)
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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.
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