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Article Dans Une Revue Nucleic Acids Research Année : 2007

Ribosomal protein S1 influences trans-translation in vitro and in vivo.

Matthieu Saguy
  • Fonction : Auteur
Reynald Gillet
  • Fonction : Auteur
Patricia Skorski
  • Fonction : Auteur
Brice Felden

Résumé

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.

Dates et versions

hal-00194443 , version 1 (06-12-2007)

Identifiants

Citer

Matthieu Saguy, Reynald Gillet, Patricia Skorski, Sylvie Hermann-Le Denmat, Brice Felden. Ribosomal protein S1 influences trans-translation in vitro and in vivo.. Nucleic Acids Research, 2007, 35 (7), pp.2368-76. ⟨10.1093/nar/gkm100⟩. ⟨hal-00194443⟩
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