ArticleScience (New York, N.Y.)2012
Structural basis for the rescue of stalled ribosomes: structure of YaeJ bound to the ribosome.
Article in Science (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
What it found
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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
62 citing papers in PubMed, 115 citations in OpenAlex.
- Molecular and structural basis of a subfamily of PrfH rescuing both the damaged and intact ribosomes stalled in translation.Science advances · 2026Article
- Knockout of the mitoribosome rescue factors Ict1 or Mtrfr is viable in zebrafish but not mice: compensatory mechanisms underlying each factor's loss.FEBS open bio · 2025Article
- Evaluating the feasibility of gene replacement strategies to treat MTRFR deficiency.Disease models & mechanisms · 2025Article
- Stalled ribosome rescue factors exert different roles depending on types of antibiotics in Escherichia coli.npj antimicrobials and resistance · 2024Article
- Mitochondrial protein synthesis quality control.Human molecular genetics · 2024Review
- Mechanistic insights into the alternative ribosome recycling by HflXr.Nucleic acids research · 2024Article
- Gene Networks Analysis ofIranian journal of biotechnology · 2023Article
- Nonstop mRNAs generate a ground state of mitochondrial gene expression noise.Science advances · 2022Article
- Sequential rescue and repair of stalled and damaged ribosome by bacterial PrfH and RtcB.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Bacterial Ribosome Rescue Systems.Microorganisms · 2022Review
- Maintaining mitochondrial ribosome function: The role of ribosome rescue and recycling factors.RNA biology · 2022Review
- Mechanisms of ribosome recycling in bacteria and mitochondria: a structural perspective.RNA biology · 2022Review
- Diversity and Similarity of Termination and Ribosome Rescue in Bacterial, Mitochondrial, and Cytoplasmic Translation.Biochemistry. Biokhimiia · 2021Review
- A stalled-ribosome rescue factor Pth3 is required for mitochondrial translation against antibiotics in Saccharomyces cerevisiae.Communications biology · 2021Article
- Ribosome Rescue Pathways in Bacteria.Frontiers in microbiology · 2021Review
- Dual function of GTPBP6 in biogenesis and recycling of human mitochondrial ribosomes.Nucleic acids research · 2020Article
- ArfB can displace mRNA to rescue stalled ribosomes.Nature communications · 2020Article
- Article
- Mechanism of ribosome rescue by alternative ribosome-rescue factor B.Nature communications · 2020Article
- Mechanism of ribosome shutdown by RsfS in Staphylococcus aureus revealed by integrative structural biology approach.Nature communications · 2020Article
2 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In bacteria, the hybrid transfer-messenger RNA (tmRNA) rescues ribosomes stalled on defective messenger RNAs (mRNAs). However, certain gram-negative bacteria have evolved proteins that are capable of rescuing stalled ribosomes in a tmRNA-independent manner. Here, we report a 3.2 angstrom-resolution crystal structure of the rescue factor YaeJ bound to the Thermus thermophilus 70S ribosome in complex with the initiator tRNA(i)(fMet) and a short mRNA. The structure reveals that the C-terminal tail of YaeJ functions as a sensor to discriminate between stalled and actively translating ribosomes by binding in the mRNA entry channel downstream of the A site between the head and shoulder of the 30S subunit. This allows the N-terminal globular domain to sample different conformations, so that its conserved GGQ motif is optimally positioned to catalyze the hydrolysis of peptidyl-tRNA. This structure gives insights into the mechanism of YaeJ function and provides a basis for understanding how it rescues stalled ribosomes.
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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.