ArticleNature communications2021
Structures of tmRNA and SmpB as they transit through the ribosome.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
28 citing papers in PubMed.
- Ribosomal protein bL27 protects translating ribosomes from tmRNA-SmpB.Science advances · 2026Article
- Multi-site DMS probing reveals higher-order structure of RNA-protein complexes in living cells.Molecular cell · 2026Article
- Molecular and structural basis of a subfamily of PrfH rescuing both the damaged and intact ribosomes stalled in translation.Science advances · 2026Article
- Ribosomal Protein bL27 Protects Translating Ribosomes from tmRNA-SmpB.bioRxiv : the preprint server for biology · 2026Article
- Translation quality control in Pseudomonas aeruginosa: current knowledge and perspectives.FEMS microbiology reviews · 2026Review
- IscR-tmRNA regulatory axis plays a key role in multiple stress response and pathogenicity inVirulence · 2025Article
- Carrot and stick: how RNase R contributes to function and destruction of the translation machinery.RNA biology · 2025Review
- Exploring Metalloproteome Remodeling in Calprotectin-StressedACS chemical biology · 2025Article
- AJournal of bacteriology · 2025Article
- Exploring metalloproteome remodeling in calprotectin-stressedbioRxiv : the preprint server for biology · 2025Article
- The ubiquitous pyridoxal 5'-phosphate-binding protein is also an RNA-binding protein.Protein science : a publication of the Protein Society · 2024Article
- Structural basis of MALAT1 RNA maturation and mascRNA biogenesis.Nature structural & molecular biology · 2024Article
- Stalled ribosome rescue factors exert different roles depending on types of antibiotics in Escherichia coli.npj antimicrobials and resistance · 2024Article
- Alternate conformational trajectories in ribosome translocation.PLoS computational biology · 2024Article
- The Beak of Eukaryotic Ribosomes: Life, Work and Miracles.Biomolecules · 2024Review
- Structural basis of translation inhibition by a valine tRNA-derived fragment.Life science alliance · 2024Article
- Article
- The Structural and Molecular Mechanisms ofMolecules (Basel, Switzerland) · 2024Review
- Editorial: tRNA and protein synthesis in microorganisms.Frontiers in microbiology · 2024Article
- Endogenous trans-translation structure visualizes the decoding of the first tmRNA alanine codon.Frontiers in microbiology · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In bacteria, trans-translation is the main rescue system, freeing ribosomes stalled on defective messenger RNAs. This mechanism is driven by small protein B (SmpB) and transfer-messenger RNA (tmRNA), a hybrid RNA known to have both a tRNA-like and an mRNA-like domain. Here we present four cryo-EM structures of the ribosome during trans-translation at resolutions from 3.0 to 3.4 Å. These include the high-resolution structure of the whole pre-accommodated state, as well as structures of the accommodated state, the translocated state, and a translocation intermediate. Together, they shed light on the movements of the tmRNA-SmpB complex in the ribosome, from its delivery by the elongation factor EF-Tu to its passage through the ribosomal A and P sites after the opening of the B1 bridges. Additionally, we describe the interactions between the tmRNA-SmpB complex and the ribosome. These explain why the process does not interfere with canonical translation.
Indexed as
Identifiers
What OpenQuestion holds
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.