Structures of tmRNA and SmpB as they transit through the ribosome

Charlotte Guyomar, Gaetano D’Urso, Sophie Chat, Emmanuel Giudice () and Reynald Gillet ()
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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

Nature Communications, 2021, vol. 12, issue 1, 1-14

Abstract: 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.

Date: 2021
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-24881-4

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DOI: 10.1038/s41467-021-24881-4

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