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Structures of tmRNA and SmpB as they transit through the ribosome

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  • Charlotte Guyomar

    (Univ. Rennes, CNRS, Institut de Génétique et Développement de Rennes (IGDR) UMR 6290)

  • Gaetano D’Urso

    (Univ. Rennes, CNRS, Institut de Génétique et Développement de Rennes (IGDR) UMR 6290)

  • Sophie Chat

    (Univ. Rennes, CNRS, Institut de Génétique et Développement de Rennes (IGDR) UMR 6290)

  • Emmanuel Giudice

    (Univ. Rennes, CNRS, Institut de Génétique et Développement de Rennes (IGDR) UMR 6290)

  • Reynald Gillet

    (Univ. Rennes, CNRS, Institut de Génétique et Développement de Rennes (IGDR) UMR 6290)

Abstract

In bacteria, trans-translation is the main rescue system, freeing ribosomes stalled on defective messenger RNAs. This mechanism is driven by small protein B (SmpB) and transfer-messenger RNA (tmRNA), a hybrid RNA known to have both a tRNA-like and an mRNA-like domain. Here we present four cryo-EM structures of the ribosome during trans-translation at resolutions from 3.0 to 3.4 Å. These include the high-resolution structure of the whole pre-accommodated state, as well as structures of the accommodated state, the translocated state, and a translocation intermediate. Together, they shed light on the movements of the tmRNA-SmpB complex in the ribosome, from its delivery by the elongation factor EF-Tu to its passage through the ribosomal A and P sites after the opening of the B1 bridges. Additionally, we describe the interactions between the tmRNA-SmpB complex and the ribosome. These explain why the process does not interfere with canonical translation.

Suggested Citation

  • Charlotte Guyomar & Gaetano D’Urso & Sophie Chat & Emmanuel Giudice & Reynald Gillet, 2021. "Structures of tmRNA and SmpB as they transit through the ribosome," Nature Communications, Nature, vol. 12(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24881-4
    DOI: 10.1038/s41467-021-24881-4
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