UPF1-like helicase grip on nucleic acids dictates processivity

Joanne Kanaan, Saurabh Raj, Laurence Decourty, Cosmin Saveanu, Vincent Croquette () and Hervé Le Hir ()
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Joanne Kanaan: PSL Research University
Saurabh Raj: PSL Research University
Laurence Decourty: Institut Pasteur
Cosmin Saveanu: Institut Pasteur
Vincent Croquette: PSL Research University
Hervé Le Hir: PSL Research University

Nature Communications, 2018, vol. 9, issue 1, 1-9

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-06313-y

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