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Cryo-EM structure of Hepatitis C virus IRES bound to the human ribosome at 3.9-Å resolution

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Listed:
  • Nick Quade

    (Institute of Molecular Biology and Biophysics)

  • Daniel Boehringer

    (Institute of Molecular Biology and Biophysics)

  • Marc Leibundgut

    (Institute of Molecular Biology and Biophysics)

  • Joop van den Heuvel

    (Research Group Recombinant Protein Expression, Helmholtz Centre for Infection Research)

  • Nenad Ban

    (Institute of Molecular Biology and Biophysics)

Abstract

Hepatitis C virus (HCV), a widespread human pathogen, is dependent on a highly structured 5′-untranslated region of its mRNA, referred to as internal ribosome entry site (IRES), for the translation of all of its proteins. The HCV IRES initiates translation by directly binding to the small ribosomal subunit (40S), circumventing the need for many eukaryotic translation initiation factors required for mRNA scanning. Here we present the cryo-EM structure of the human 40S ribosomal subunit in complex with the HCV IRES at 3.9 Å resolution, determined by focused refinement of an 80S ribosome–HCV IRES complex. The structure reveals the molecular details of the interactions between the IRES and the 40S, showing that expansion segment 7 (ES7) of the 18S rRNA acts as a central anchor point for the HCV IRES. The structural data rationalizes previous biochemical and genetic evidence regarding the initiation mechanism of the HCV and other related IRESs.

Suggested Citation

  • Nick Quade & Daniel Boehringer & Marc Leibundgut & Joop van den Heuvel & Nenad Ban, 2015. "Cryo-EM structure of Hepatitis C virus IRES bound to the human ribosome at 3.9-Å resolution," Nature Communications, Nature, vol. 6(1), pages 1-9, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8646
    DOI: 10.1038/ncomms8646
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    Cited by:

    1. Georg Dorn & Christoph Gmeiner & Tebbe Vries & Emil Dedic & Mihajlo Novakovic & Fred F. Damberger & Christophe Maris & Esteban Finol & Chris P. Sarnowski & Joachim Kohlbrecher & Timothy J. Welsh & Sre, 2023. "Integrative solution structure of PTBP1-IRES complex reveals strong compaction and ordering with residual conformational flexibility," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    2. Shivali Patel & Alec N. Sexton & Madison S. Strine & Craig B. Wilen & Matthew D. Simon & Anna Marie Pyle, 2023. "Systematic detection of tertiary structural modules in large RNAs and RNP interfaces by Tb-seq," Nature Communications, Nature, vol. 14(1), pages 1-11, December.

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