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A ratchet-like inter-subunit reorganization of the ribosome during translocation

Author

Listed:
  • Joachim Frank

    (Howard Hughes Medical Institute,
    Health Research Incorporated at the Wadsworth Center
    State University of New York at Albany)

  • Rajendra Kumar Agrawal

    (Health Research Incorporated at the Wadsworth Center
    State University of New York at Albany)

Abstract

The ribosome is a macromolecular assembly that is responsible for protein biosynthesis following genetic instructions in all organisms. It is composed of two unequal subunits: the smaller subunit binds messenger RNA and the anticodon end of transfer RNAs, and helps to decode the mRNA; and the larger subunit interacts with the amino-acid-carrying end of tRNAs and catalyses the formation of the peptide bonds. After peptide-bond formation, elongation factor G (EF-G) binds to the ribosome, triggering the translocation of peptidyl-tRNA from its aminoacyl site to the peptidyl site, and movement of mRNA by one codon1. Here we analyse three-dimensional cryo-electron microscopy maps of the Escherichia coli 70S ribosome in various functional states, and show that both EF-G binding and subsequent GTP hydrolysis lead to ratchet-like rotations of the small 30S subunit relative to the large 50S subunit. Furthermore, our finding indicates a two-step mechanism of translocation: first, relative rotation of the subunits and opening of the mRNA channel following binding of GTP to EF-G; and second, advance of the mRNA/(tRNA)2 complex in the direction of the rotation of the 30S subunit, following GTP hydrolysis.

Suggested Citation

  • Joachim Frank & Rajendra Kumar Agrawal, 2000. "A ratchet-like inter-subunit reorganization of the ribosome during translocation," Nature, Nature, vol. 406(6793), pages 318-322, July.
    • Handle: RePEc:nat:nature:v:406:y:2000:i:6793:d:10.1038_35018597
    DOI: 10.1038/35018597
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    Cited by:

    1. Chen Bao & Mingyi Zhu & Inna Nykonchuk & Hironao Wakabayashi & David H. Mathews & Dmitri N. Ermolenko, 2022. "Specific length and structure rather than high thermodynamic stability enable regulatory mRNA stem-loops to pause translation," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    2. Panagiotis Poulis & Anoshi Patel & Marina V. Rodnina & Sarah Adio, 2022. "Altered tRNA dynamics during translocation on slippery mRNA as determinant of spontaneous ribosome frameshifting," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    3. Christine E. Carbone & Anna B. Loveland & Howard B. Gamper & Ya-Ming Hou & Gabriel Demo & Andrei A. Korostelev, 2021. "Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    4. Sergio Cruz-León & Tomáš Majtner & Patrick C. Hoffmann & Jan Philipp Kreysing & Sebastian Kehl & Maarten W. Tuijtel & Stefan L. Schaefer & Katharina Geißler & Martin Beck & Beata Turoňová & Gerhard Hu, 2024. "High-confidence 3D template matching for cryo-electron tomography," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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