ArticleNature2017
Structural basis for ArfA-RF2-mediated translation termination on mRNAs lacking stop codons.
Article in Nature, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 56 citations in OpenAlex.
- Translation as a regulatory hub for secondary metabolism in Streptomyces spp.Essays in biochemistry · 2026Review
- Developing the protein quality control system inSynthetic and systems biotechnology · 2026Article
- Molecular and structural basis of a subfamily of PrfH rescuing both the damaged and intact ribosomes stalled in translation.Science advances · 2026Article
- A cascade of structural rearrangements positions peptide release factor 2 for polypeptide hydrolysis on the ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Improving polyketide biosynthesis by rescuing the translation of truncated mRNAs into functional polyketide synthase subunits.Nature communications · 2025Article
- Stalled ribosome rescue factors exert different roles depending on types of antibiotics in Escherichia coli.npj antimicrobials and resistance · 2024Article
- The Structural and Molecular Mechanisms ofMolecules (Basel, Switzerland) · 2024Review
- Mechanistic insights into the alternative ribosome recycling by HflXr.Nucleic acids research · 2024Article
- A kinetic model for solving a combination optimization problem in ab-initio Cryo-EM 3D reconstruction.Briefings in bioinformatics · 2024Article
- Prophage excision switches the primary ribosome rescue pathway and rescue-associated gene regulations in Escherichia coli.Molecular microbiology · 2023Article
- 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
- Ribosome-associated quality-control mechanisms from bacteria to humans.Molecular cell · 2022Review
- 3D reconstruction from cryo-EM projection images using two spherical embeddings.Communications biology · 2022Article
- Bacterial Ribosome Rescue Systems.Microorganisms · 2022Review
- Maintaining mitochondrial ribosome function: The role of ribosome rescue and recycling factors.RNA biology · 2022Review
- Structural basis of l-tryptophan-dependent inhibition of release factor 2 by the TnaC arrest peptide.Nucleic acids research · 2021Article
- Diversity and Similarity of Termination and Ribosome Rescue in Bacterial, Mitochondrial, and Cytoplasmic Translation.Biochemistry. Biokhimiia · 2021Review
- In silico analysis of bacterial translation factors reveal distinct translation event specific pI values.BMC genomics · 2021Article
- Ribosome Rescue Pathways in Bacteria.Frontiers in microbiology · 2021Review
- ArfB can displace mRNA to rescue stalled ribosomes.Nature communications · 2020Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In bacteria, ribosomes stalled on truncated mRNAs that lack a stop codon are rescued by the transfer-messenger RNA (tmRNA), alternative rescue factor A (ArfA) or ArfB systems. Although tmRNA-ribosome and ArfB-ribosome structures have been determined, how ArfA recognizes the presence of truncated mRNAs and recruits the canonical termination release factor RF2 to rescue the stalled ribosomes is unclear. Here we present a cryo-electron microscopy reconstruction of the Escherichia coli 70S ribosome stalled on a truncated mRNA in the presence of ArfA and RF2. The structure shows that the C terminus of ArfA binds within the mRNA entry channel on the small ribosomal subunit, and explains how ArfA distinguishes between ribosomes that bear truncated or full-length mRNAs. The N terminus of ArfA establishes several interactions with the decoding domain of RF2, and this finding illustrates how ArfA recruits RF2 to the stalled ribosome. Furthermore, ArfA is shown to stabilize a unique conformation of the switch loop of RF2, which mimics the canonical translation termination state by directing the catalytically important GGQ motif within domain 3 of RF2 towards the peptidyl-transferase centre of the ribosome. Thus, our structure reveals not only how ArfA recruits RF2 to the ribosome but also how it promotes an active conformation of RF2 to enable translation termination in the absence of a stop codon.
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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.