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Human Upf1 is a highly processive RNA helicase and translocase with RNP remodelling activities

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  • Francesca Fiorini

    (Institut de Biologie de l’Ecole Normale Supérieure, CNRS UMR8197
    Institut de Biologie de l’Ecole Normale Supérieure, INSERM U1024)

  • Debjani Bagchi

    (Institut de Biologie de l’Ecole Normale Supérieure, CNRS UMR8197
    Institut de Biologie de l’Ecole Normale Supérieure, INSERM U1024
    Laboratoire de Physique Statistique, Ecole Normale Supérieure, Université Pierre et Marie Curie Paris, Université Paris Diderot
    Present address: Physics Department, Faculty of Science, The M.S. University of Baroda, Vadodara 390002, Gujarat, India.)

  • Hervé Le Hir

    (Institut de Biologie de l’Ecole Normale Supérieure, CNRS UMR8197
    Institut de Biologie de l’Ecole Normale Supérieure, INSERM U1024)

  • Vincent Croquette

    (Institut de Biologie de l’Ecole Normale Supérieure, CNRS UMR8197
    Institut de Biologie de l’Ecole Normale Supérieure, INSERM U1024
    Laboratoire de Physique Statistique, Ecole Normale Supérieure, Université Pierre et Marie Curie Paris, Université Paris Diderot)

Abstract

RNA helicases are implicated in most cellular RNA-dependent events. In eukaryotes however, only few have been functionally characterized. Upf1 is a RNA helicase essential for nonsense-mediated mRNA decay (NMD). Here, using magnetic tweezers and bulk assays, we observe that human Upf1 is able to translocate slowly over long single-stranded nucleic acids with a processivity >10 kb. Upf1 efficiently translocates through double-stranded structures and protein-bound sequences, demonstrating that Upf1 is an efficient ribonucleoprotein complex remodeler. Our observation of processive unwinding by an eukaryotic RNA helicase reveals that Upf1, once recruited onto NMD mRNA targets, can scan the entire transcript to irreversibly remodel the mRNP, facilitating its degradation by the NMD machinery.

Suggested Citation

  • Francesca Fiorini & Debjani Bagchi & Hervé Le Hir & Vincent Croquette, 2015. "Human Upf1 is a highly processive RNA helicase and translocase with RNP remodelling activities," Nature Communications, Nature, vol. 6(1), pages 1-10, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8581
    DOI: 10.1038/ncomms8581
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