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Mechanism of ribosome rescue by alternative ribosome-rescue factor B

Author

Listed:
  • Kai-Hsin Chan

    (Max Planck Institute for Biophysical Chemistry)

  • Valentyn Petrychenko

    (Max Planck Institute for Biophysical Chemistry)

  • Claudia Mueller

    (University of Hamburg)

  • Cristina Maracci

    (Max Planck Institute for Biophysical Chemistry)

  • Wolf Holtkamp

    (Max Planck Institute for Biophysical Chemistry
    Paul-Ehrlich-Institut)

  • Daniel N. Wilson

    (University of Hamburg)

  • Niels Fischer

    (Max Planck Institute for Biophysical Chemistry)

  • Marina V. Rodnina

    (Max Planck Institute for Biophysical Chemistry)

Abstract

Alternative ribosome-rescue factor B (ArfB) rescues ribosomes stalled on non-stop mRNAs by releasing the nascent polypeptide from the peptidyl-tRNA. By rapid kinetics we show that ArfB selects ribosomes stalled on short truncated mRNAs, rather than on longer mRNAs mimicking pausing on rare codon clusters. In combination with cryo-electron microscopy we dissect the multistep rescue pathway of ArfB, which first binds to ribosomes very rapidly regardless of the mRNA length. The selectivity for shorter mRNAs arises from the subsequent slow engagement step, as it requires longer mRNA to shift to enable ArfB binding. Engagement results in specific interactions of the ArfB C-terminal domain with the mRNA entry channel, which activates peptidyl-tRNA hydrolysis by the N-terminal domain. These data reveal how protein dynamics translate into specificity of substrate recognition and provide insights into the action of a putative rescue factor in mitochondria.

Suggested Citation

  • Kai-Hsin Chan & Valentyn Petrychenko & Claudia Mueller & Cristina Maracci & Wolf Holtkamp & Daniel N. Wilson & Niels Fischer & Marina V. Rodnina, 2020. "Mechanism of ribosome rescue by alternative ribosome-rescue factor B," Nature Communications, Nature, vol. 11(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17853-7
    DOI: 10.1038/s41467-020-17853-7
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    Cited by:

    1. Franziska Nadler & Elena Lavdovskaia & Angelique Krempler & Luis Daniel Cruz-Zaragoza & Sven Dennerlein & Ricarda Richter-Dennerlein, 2022. "Human mtRF1 terminates COX1 translation and its ablation induces mitochondrial ribosome-associated quality control," Nature Communications, Nature, vol. 13(1), pages 1-10, December.

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