In vivo tmRNA protection by SmpB and pre-ribosome binding conformation in solution.

Abstract : TmRNA is an abundant RNA in bacteria with tRNA and mRNA features. It is specialized in trans-translation, a translation rescuing system. We demonstrate that its partner protein SmpB binds the tRNA-like region (TLD) in vivo and chaperones the fold of the TLD-H2 region. We use an original approach combining the observation of tmRNA degradation pathways in a heterologous system, the analysis of the tmRNA digests by MS and NMR, and co-overproduction assays of tmRNA and SmpB. We study the conformation in solution of tmRNA alone or in complex with one SmpB before ribosome binding using SAXS. Our data show that Mg(2+) drives compaction of the RNA structure and that, in the absence of Mg(2+), SmpB has a similar effect albeit to a lesser extent. Our results show that tmRNA is intrinsically structured in solution with identical topology to that observed on complexes on ribosomes which should facilitate its subsequent recruitment by the 70S ribosome, free or preloaded with one SmpB molecule.
Type de document :
Article dans une revue
RNA, Cold Spring Harbor Laboratory Press, 2014, 20 (10), pp.1607-20. 〈10.1261/rna.045674.114〉
Liste complète des métadonnées

https://hal.inria.fr/hal-01058972
Contributeur : Julie Bernauer <>
Soumis le : jeudi 28 août 2014 - 20:19:37
Dernière modification le : jeudi 10 mai 2018 - 02:06:01

Lien texte intégral

Identifiants

Citation

Ehsan Ranaei-Siadat, Cécile Mérigoux, Bili Seijo, Luc Ponchon, Jean-Michel Saliou, et al.. In vivo tmRNA protection by SmpB and pre-ribosome binding conformation in solution.. RNA, Cold Spring Harbor Laboratory Press, 2014, 20 (10), pp.1607-20. 〈10.1261/rna.045674.114〉. 〈hal-01058972〉

Partager

Métriques

Consultations de la notice

463