Skip to Main content Skip to Navigation
Journal articles

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

Abstract : 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 DeltasmpB 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.
Document type :
Journal articles
Complete list of metadatas

Cited literature [22 references]  Display  Hide  Download

https://www.hal.inserm.fr/inserm-00706654
Contributor : Annick Lefevre <>
Submitted on : Monday, June 11, 2012 - 11:49:37 AM
Last modification on : Friday, March 27, 2020 - 2:19:51 AM
Long-term archiving on: : Wednesday, September 12, 2012 - 2:26:04 AM

File

embor2008243.pdf
Publisher files allowed on an open archive

Identifiers

Citation

Sylvie Nonin-Lecomte, Noella Germain-Amiot, Reynald Gillet, Marc Hallier, Luc Ponchon, et al.. Ribosome hijacking: a role for small protein B during trans-translation.. EMBO Reports, EMBO Press, 2009, 10 (2), pp.160-5. ⟨10.1038/embor.2008.243⟩. ⟨inserm-00706654⟩

Share

Metrics

Record views

530

Files downloads

909