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Structural basis for clearing of ribosome collisions by the RQT complex

Author

Listed:
  • Katharina Best

    (University of Munich)

  • Ken Ikeuchi

    (University of Munich)

  • Lukas Kater

    (University of Munich
    Friedrich Miescher Institute for Biomedical Research)

  • Daniel Best

    (University of Munich)

  • Joanna Musial

    (University of Munich)

  • Yoshitaka Matsuo

    (The University of Tokyo)

  • Otto Berninghausen

    (University of Munich)

  • Thomas Becker

    (University of Munich)

  • Toshifumi Inada

    (The University of Tokyo)

  • Roland Beckmann

    (University of Munich)

Abstract

Translation of aberrant messenger RNAs can cause stalling of ribosomes resulting in ribosomal collisions. Collided ribosomes are specifically recognized to initiate stress responses and quality control pathways. Ribosome-associated quality control facilitates the degradation of incomplete translation products and requires dissociation of the stalled ribosomes. A central event is therefore the splitting of collided ribosomes by the ribosome quality control trigger complex, RQT, by an unknown mechanism. Here we show that RQT requires accessible mRNA and the presence of a neighboring ribosome. Cryogenic electron microscopy of RQT-ribosome complexes reveals that RQT engages the 40S subunit of the lead ribosome and can switch between two conformations. We propose that the Ski2-like helicase 1 (Slh1) subunit of RQT applies a pulling force on the mRNA, causing destabilizing conformational changes of the small ribosomal subunit, ultimately resulting in subunit dissociation. Our findings provide conceptual framework for a helicase-driven ribosomal splitting mechanism.

Suggested Citation

  • Katharina Best & Ken Ikeuchi & Lukas Kater & Daniel Best & Joanna Musial & Yoshitaka Matsuo & Otto Berninghausen & Thomas Becker & Toshifumi Inada & Roland Beckmann, 2023. "Structural basis for clearing of ribosome collisions by the RQT complex," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
  • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-36230-8
    DOI: 10.1038/s41467-023-36230-8
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