ReviewFrontiers in microbiology2014
The SmpB C-terminal tail helps tmRNA to recognize and enter stalled ribosomes.
Review in Frontiers in microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
8 citing papers in PubMed, 13 citations in OpenAlex.
- Cooperative and Independent Functionality of tmRNA and SmpB inInternational journal of molecular sciences · 2025Article
- Trends and Implications of Ribosome-associated Protein Quality Control in Diseases: A Bibliographic Analysis.Current medicinal chemistry · 2025Review
- Article
- RqcH supports survival in the absence of non-stop ribosome rescue factors.bioRxiv : the preprint server for biology · 2024Article
- Intermolecular Communication inFrontiers in molecular biosciences · 2020Review
- Kinetic modeling predicts a stimulatory role for ribosome collisions at elongation stall sites in bacteria.eLife · 2017Article
- Ribosome pausing, arrest and rescue in bacteria and eukaryotes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2017Review
- Ribosomal frameshifting and transcriptional slippage: From genetic steganography and cryptography to adventitious use.Nucleic acids research · 2016Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
In bacteria, transfer-messenger RNA (tmRNA) and SmpB comprise the most common and effective system for rescuing stalled ribosomes. Ribosomes stall on mRNA transcripts lacking stop codons and are rescued as the defective mRNA is swapped for the tmRNA template in a process known as trans-translation. The tmRNA-SmpB complex is recruited to the ribosome independent of a codon-anticodon interaction. Given that the ribosome uses robust discriminatory mechanisms to select against non-cognate tRNAs during canonical decoding, it has been hard to explain how this can happen. Recent structural and biochemical studies show that SmpB licenses tmRNA entry through its interactions with the decoding center and mRNA channel. In particular, the C-terminal tail of SmpB promotes both EFTu activation and accommodation of tmRNA, the former through interactions with 16S rRNA nucleotide G530 and the latter through interactions with the mRNA channel downstream of the A site. Here we present a detailed model of the earliest steps in trans-translation, and in light of these mechanistic considerations, revisit the question of how tmRNA preferentially reacts with stalled, non-translating ribosomes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.