Ribosome hijacking: a role for small protein B during trans-translation - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue EMBO Reports Année : 2009

Ribosome hijacking: a role for small protein B during trans-translation

Résumé

Tight recognition of codon–anticodon pairings by the ribosome ensures the accuracy and fidelity of protein synthesis. In eubacteria, translational surveillance and ribosome rescue are performed by the ‘tmRNA–SmpB’ system (transfer messenger RNA–small protein B). Remarkably, entry and accommodation of aminoacylated-tmRNA into stalled ribosomes occur without a codon–anticodon interaction but in the presence of SmpB. Here, we show that within a stalled ribosome, SmpB interacts with the three universally conserved bases G530, A1492 and A1493 that form the 30S subunit decoding centre, in which canonical codon–anticodon pairing occurs. The footprints at positions A1492 and A1493 of a small decoding centre, as well as on a set of conserved SmpB amino acids, were identified by nuclear magnetic resonance. Mutants at these residues display the same growth defects as for ΔsmpB strains. The SmpB protein has functional and structural similarities with initiation factor 1, and is proposed to be a functional mimic of the pairing between a codon and an anticodon.
Fichier principal
Vignette du fichier
NoninEmboRev1et fig.pdf (7.31 Mo) Télécharger le fichier
NoninSupplMat.pdf (2.5 Mo) Télécharger le fichier
Origine : Fichiers produits par l'(les) auteur(s)

Dates et versions

hal-02344654 , version 1 (06-09-2021)

Identifiants

Citer

Sylvie Nonin-Lecomte, Noëlla Germain-Amiot, Reynald Gillet, Marc Hallier, Luc Ponchon, et al.. Ribosome hijacking: a role for small protein B during trans-translation. EMBO Reports, 2009, 10 (2), pp.160-165. ⟨10.1038/embor.2008.243⟩. ⟨hal-02344654⟩
53 Consultations
19 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More