Nucleic Acids Research Advance Access originally published online on March 28, 2007
Nucleic Acids Research 2007 35(7):2368-2376; doi:10.1093/nar/gkm100
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Nucleic Acids Research, 2007, Vol. 35, No. 7 2368-2376
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Ribosomal protein S1 influences trans-translation in vitro and in vivo
1Université de Rennes 1, UPRES 2311, Inserm U835, Biochimie Pharmaceutique, 2 Avenue du Prof. Léon Bernard, 35000 Rennes, France and 2Laboratoire de Génétique Moléculaire, CNRS UMR8541, Ecole Normale Supérieure, 46 Rue d’Ulm, 75230 Paris, France
*To whom correspondence should be addressed. Tel: +33 2 23 23 48 51; Fax: 33 2 23 23 44 56; Email: bfelden{at}univ-rennes1.fr
Received November 20, 2006. Revised February 2, 2007. Accepted February 5, 2007.
When the bacterial ribosome stalls on a truncated mRNA, transfer–messenger RNA (tmRNA) acts initially as a transfer RNA (tRNA) and then as a messenger RNA (mRNA) to rescue the ribosome and add a peptide tag to the nascent polypeptide that targets it for degradation. Ribosomal protein S1 binds tmRNA but its functional role in this process has remained elusive. In this report, we demonstrate that, in vitro, S1 is dispensable for the tRNA-like role of tmRNA but is essential for its mRNA function. Increasing or decreasing the amount of protein S1 in vivo reduces the overall amount of trans-translated proteins. Also, a truncated S1 protein impaired for ribosome binding can still trigger protein tagging, suggesting that S1 interacts with tmRNA outside the ribosome to keep it in an active state. Overall, these results demonstrate that S1 has a role in tmRNA-mediated tagging that is distinct from its role during canonical translation.
Present address: Univ Paris-Sud, Institut de Génétique et Microbiologie-CNRS UMR8621, Orsay, F-91405
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