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Pre-binding of Small Protein B to a Stalled Ribosome Triggers trans-Translation

To rescue stalled ribosomes, eubacteria employ a molecule, transfer messenger RNA (tmRNA), which functions both as a tRNA and as an mRNA. With the help of small protein B (SmpB), tmRNA restarts protein synthesis and adds by the trans-translation mechanism a peptide tag to the stalled protein to targ...

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Bibliographic Details
Published in:The Journal of biological chemistry 2004-06, Vol.279 (25), p.25978-25985
Main Authors: Hallier, Marc, Ivanova, Natalia, Rametti, Armelle, Pavlov, Michael, Ehrenberg, Måns, Felden, Brice
Format: Article
Language:English
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Summary:To rescue stalled ribosomes, eubacteria employ a molecule, transfer messenger RNA (tmRNA), which functions both as a tRNA and as an mRNA. With the help of small protein B (SmpB), tmRNA restarts protein synthesis and adds by the trans-translation mechanism a peptide tag to the stalled protein to target it for destruction by cellular proteases. Here, the cellular location and expression of endogenous SmpB were monitored in vivo. We report that SmpB is associated with 70S ribosomes and not in the soluble fraction, independently of the presence of tmRNA. In vitro, SmpB that is pre-bound to a stalled ribosome can trigger initiation of trans-translation. Our results demonstrate the existence of a novel pathway for the entry of tmRNA to the ribosome and for the trans-transfer of a nascent peptide chain from peptidyl-tRNA to charged tmRNA.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M314086200