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The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy

Author

Listed:
  • Ziao Fu

    (Columbia University)

  • Gabriele Indrisiunaite

    (Uppsala University)

  • Sandip Kaledhonkar

    (Columbia University)

  • Binita Shah

    (Barnard College)

  • Ming Sun

    (Columbia University)

  • Bo Chen

    (Columbia University)

  • Robert A. Grassucci

    (Columbia University)

  • Måns Ehrenberg

    (Uppsala University)

  • Joachim Frank

    (Columbia University
    Columbia University)

Abstract

When the ribosome encounters a stop codon, it recruits a release factor (RF) to hydrolyze the ester bond between the peptide chain and tRNA. RFs have structural motifs that recognize stop codons in the decoding center and a GGQ motif for induction of hydrolysis in the peptidyl transfer center 70 Å away. Surprisingly, free RF2 is compact, with only 20 Å between its codon-reading and GGQ motifs. Cryo-EM showed that ribosome-bound RFs have extended structures, suggesting that RFs are compact when entering the ribosome and then extend their structures upon stop codon recognition. Here we use time-resolved cryo-EM to visualize transient compact forms of RF1 and RF2 at 3.5 and 4 Å resolution, respectively, in the codon-recognizing ribosome complex on the native pathway. About 25% of complexes have RFs in the compact state at 24 ms reaction time, and within 60 ms virtually all ribosome-bound RFs are transformed to their extended forms.

Suggested Citation

  • Ziao Fu & Gabriele Indrisiunaite & Sandip Kaledhonkar & Binita Shah & Ming Sun & Bo Chen & Robert A. Grassucci & Måns Ehrenberg & Joachim Frank, 2019. "The structural basis for release-factor activation during translation termination revealed by time-resolved cryogenic electron microscopy," Nature Communications, Nature, vol. 10(1), pages 1-7, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10608-z
    DOI: 10.1038/s41467-019-10608-z
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    Cited by:

    1. Timo Flügel & Magdalena Schacherl & Anett Unbehaun & Birgit Schroeer & Marylena Dabrowski & Jörg Bürger & Thorsten Mielke & Thiemo Sprink & Christoph A. Diebolder & Yollete V. Guillén Schlippe & Chris, 2024. "Transient disome complex formation in native polysomes during ongoing protein synthesis captured by cryo-EM," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    2. Narayan Prasad Parajuli & Andrew Emmerich & Chandra Sekhar Mandava & Michael Y. Pavlov & Suparna Sanyal, 2023. "Antibiotic thermorubin tethers ribosomal subunits and impedes A-site interactions to perturb protein synthesis in bacteria," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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