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Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome

Author

Listed:
  • Marina V. Rodnina

    (University of Witten/Herdecke)

  • Andreas Savelsbergh

    (University of Witten/Herdecke)

  • Vladimir I. Katunin

    (University of Witten/Herdecke)

  • Wolfgang Wintermeyer

    (University of Witten/Herdecke)

Abstract

Elongation factor G (EF-G) is a GTPase that is involved in the translocation of bacterial ribosomes along messenger RNA during protein biosynthesis. In contrast to current models, EF-G-dependent GTP hydrolysis is shown to precede, and greatly accelerate, the rearrangement of the ribosome that leads to translocation. Domain IV of the EF-G structure is crucial for both rapid translocation and subsequent release of the factor from the ribosome. By coupling the free energy of GTP hydrolysis to translocation, EF-G serves as a motor protein to drive the directional movement of transfer and messenger RNAs on the ribosome.

Suggested Citation

  • Marina V. Rodnina & Andreas Savelsbergh & Vladimir I. Katunin & Wolfgang Wintermeyer, 1997. "Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome," Nature, Nature, vol. 385(6611), pages 37-41, January.
    • Handle: RePEc:nat:nature:v:385:y:1997:i:6611:d:10.1038_385037a0
    DOI: 10.1038/385037a0
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    Cited by:

    1. 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.
    2. 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.
    3. Valentyn Petrychenko & Bee-Zen Peng & Ana C. A. P. Schwarzer & Frank Peske & Marina V. Rodnina & Niels Fischer, 2021. "Structural mechanism of GTPase-powered ribosome-tRNA movement," Nature Communications, Nature, vol. 12(1), pages 1-9, December.

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