ArticleRNA (New York, N.Y.)2007
Structure probing of tmRNA in distinct stages of trans-translation.
Article in RNA (New York, N.Y.), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
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- Comparative Analysis Reveals Host Species-Dependent Diversity Among 16 Virulent Bacteriophages Isolated Against SoybeanbioRxiv : the preprint server for biology · 2025Article
- Led-Seq: ligation-enhanced double-end sequence-based structure analysis of RNA.Nucleic acids research · 2023Article
- Lead-seq: transcriptome-wide structure probing in vivo using lead(II) ions.Nucleic acids research · 2020Article
- tmRNA-mediated trans-translation as the major ribosome rescue system in a bacterial cell.Frontiers in genetics · 2014Review
- The tmRNA ribosome-rescue system.Advances in protein chemistry and structural biology · 2012Review
- Bifunctional transfer-messenger RNA.Biochimie · 2011Review
- tRNA/mRNA Mimicry by tmRNA and SmpB in Trans-Translation.Journal of nucleic acids · 2011Article
- Visualizing the transfer-messenger RNA as the ribosome resumes translation.The EMBO journal · 2010Article
- Structural features of the tmRNA-ribosome interaction.RNA (New York, N.Y.) · 2009Article
- Significant bias against the ACA triplet in the tmRNA sequence of Escherichia coli K-12.Journal of bacteriology · 2009Article
- SmpB contributes to reading frame selection in the translation of transfer-messenger RNA.Journal of molecular biology · 2009Article
- The role of upstream sequences in selecting the reading frame on tmRNA.BMC biology · 2008Article
- A functional interaction of SmpB with tmRNA for determination of the resuming point of trans-translation.RNA (New York, N.Y.) · 2007Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribosomes stalled on problematic mRNAs in bacterial cells can be rescued by transfer-messenger RNA (tmRNA), its helper protein (small protein B, SmpB), and elongation factor Tu (EF-Tu) through a mechanism called trans-translation. In this work we used lead(II) footprinting to probe the interactions of tmRNA with SmpB and other components of the translation machinery at different steps of the trans-translation cycle. Ribosomes with a short nascent peptide stalled on a truncated mRNA were reacted with Ala-tmRNA*EF-Tu*GTP, SmpB, and other translation components to initiate and execute trans-translation. Free tmRNA was probed with lead(II) acetate with and without SmpB, and ribosome bound tmRNA was probed in one of four different trans-translation states stabilized by antibiotic addition or selective exclusion of translation components. For comparison, we also analyzed lead(II) cleavage patterns of tmRNA in vivo in a wild-type as well as in an SmpB-deficient Escherichia coli strain. We observed some specific cleavages/protections in tmRNA for the individual steps of trans-translation, but the overall tmRNA conformation appeared to be similar in the stages analyzed. Our findings suggest that, in vivo, a dominant fraction of tmRNA is in complex with SmpB and that, in vitro, SmpB remains tmRNA bound at the initial steps of trans-translation.
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