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Nucleic Acids Research 2006 34(6):1935-1943; doi:10.1093/nar/gkl097
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Published online 12 April 2006

© The Author 2006. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org

Article

Small protein B interacts with the large and the small subunits of a stalled ribosome during trans-translation

Marc Hallier, Jessie Desreac and Brice Felden*

Université de Rennes I, Upres JE 2311, Inserm ESPRI, Biochimie Pharmaceutique 2 Avenue du Prof. Léon Bernard, 35043 Rennes, France

*To whom correspondence should be addressed. Tel: +332 2323 4851; Fax: +332 2323 4456; Email: bfelden{at}univ-rennes1.fr

Received December 19, 2005. Revised February 10, 2006. Accepted March 7, 2006.

During trans-translation, stalled bacterial ribosomes are rescued by small protein B (SmpB) and by transfer-messenger RNA (tmRNA). Stalled ribosomes switch translation from the defective messages to a short internal reading frame on tmRNA that tags the nascent peptide chain for degradation and recycles the ribosomes. We present evidences that SmpB binds the large and small ribosomal subunits in vivo and in vitro. The binding between SmpB and the ribosomal subunits is very tight, with a dissociation constant of 1.7 x 10–10 M, similar to its KD for the 70S ribosome or for tmRNA. tmRNA displaces SmpB from its 50S binding but not from the 30S. In vivo, SmpB is detected on the 50S when trans-translation is impaired by lacking tmRNA or a functional SmpB. SmpB contacts the large subunit transiently and early during the trans-translational process. The affinity of SmpB for the two ribosomal subunits is modulated by tmRNA in the course of trans-translation. It is the first example of two copies of the same protein interacting with two different functional sites of the ribosomes.


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