UPF1-like helicase grip on nucleic acids dictates processivity

Nature Communications
Joanne KanaanHervé Le Hir

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.

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Citations

Aug 21, 2019·Wiley Interdisciplinary Reviews. RNA·Donny D LicatalosiEckhard Jankowsky
Apr 18, 2019·Nature Reviews. Molecular Cell Biology·Tatsuaki KurosakiLynne E Maquat
Jul 9, 2020·Biomolecules·Daria Lavysh, Gabriele Neu-Yilik
May 28, 2019·Wiley Interdisciplinary Reviews. RNA·Aparna KishorJ Robert Hogg
Aug 12, 2019·Biophysical Journal·Shaon ChakrabartiD Thirumalai
Oct 30, 2019·Chemical Reviews·Sonisilpa MohapatraTaekjip Ha
Nov 3, 2021·Human Molecular Genetics·Caley E SmithChristian L Lorson

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Datasets Mentioned

BETA
Q92900-2

Methods Mentioned

BETA
targeted mutations
PCR
PCRs
electrophoresis

Software Mentioned

Fiji
ImageJ
SMBA

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