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ArfB can displace mRNA to rescue stalled ribosomes

Author

Listed:
  • Christine E. Carbone

    (UMass Medical School)

  • Gabriel Demo

    (UMass Medical School
    Masaryk University)

  • Rohini Madireddy

    (UMass Medical School
    Medicago Inc.)

  • Egor Svidritskiy

    (UMass Medical School
    Sanofi)

  • Andrei A. Korostelev

    (UMass Medical School)

Abstract

Ribosomes stalled during translation must be rescued to replenish the pool of translation-competent ribosomal subunits. Bacterial alternative rescue factor B (ArfB) releases nascent peptides from ribosomes stalled on mRNAs truncated at the A site, allowing ribosome recycling. Prior structural work revealed that ArfB recognizes such ribosomes by inserting its C-terminal α-helix into the vacant mRNA tunnel. In this work, we report that ArfB can efficiently recognize a wider range of mRNA substrates, including longer mRNAs that extend beyond the A-site codon. Single-particle cryo-EM unveils that ArfB employs two modes of function depending on the mRNA length. ArfB acts as a monomer to accommodate a shorter mRNA in the ribosomal A site. By contrast, longer mRNAs are displaced from the mRNA tunnel by more than 20 Å and are stabilized in the intersubunit space by dimeric ArfB. Uncovering distinct modes of ArfB function resolves conflicting biochemical and structural studies, and may lead to re-examination of other ribosome rescue pathways, whose functions depend on mRNA lengths.

Suggested Citation

  • Christine E. Carbone & Gabriel Demo & Rohini Madireddy & Egor Svidritskiy & Andrei A. Korostelev, 2020. "ArfB can displace mRNA to rescue stalled ribosomes," Nature Communications, Nature, vol. 11(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-19370-z
    DOI: 10.1038/s41467-020-19370-z
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