ArticleNature communications2020
ArfB can displace mRNA to rescue stalled ribosomes.
Article in Nature communications, 2020. 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.
- Mitochondrial translation termination, recycling, reinitiation, and rescue for in-frame and out-of-frame contexts.Nature communications · 2026Article
- Molecular and structural basis of a subfamily of PrfH rescuing both the damaged and intact ribosomes stalled in translation.Science advances · 2026Article
- Emerging mechanisms of human mitochondrial translation regulation.Trends in biochemical sciences · 2025Review
- Evaluating the feasibility of gene replacement strategies to treat MTRFR deficiency.Disease models & mechanisms · 2025Article
- Mitochondrial protein synthesis quality control.Human molecular genetics · 2024Review
- The Structural and Molecular Mechanisms ofMolecules (Basel, Switzerland) · 2024Review
- Mechanistic insights into the alternative ribosome recycling by HflXr.Nucleic acids research · 2024Article
- 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
- Diversity and Similarity of Termination and Ribosome Rescue in Bacterial, Mitochondrial, and Cytoplasmic Translation.Biochemistry. Biokhimiia · 2021Review
- Structures of tmRNA and SmpB as they transit through the ribosome.Nature communications · 2021Article
- Ribosome Rescue Pathways in Bacteria.Frontiers in microbiology · 2021Review
- Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Ribosomes stalled during translation must be rescued to replenish the pool of translation-competent ribosomal subunits. Bacterial alternative rescue factor B (ArfB) releases nascent peptides from ribosomes stalled on mRNAs truncated at the A site, allowing ribosome recycling. Prior structural work revealed that ArfB recognizes such ribosomes by inserting its C-terminal α-helix into the vacant mRNA tunnel. In this work, we report that ArfB can efficiently recognize a wider range of mRNA substrates, including longer mRNAs that extend beyond the A-site codon. Single-particle cryo-EM unveils that ArfB employs two modes of function depending on the mRNA length. ArfB acts as a monomer to accommodate a shorter mRNA in the ribosomal A site. By contrast, longer mRNAs are displaced from the mRNA tunnel by more than 20 Å and are stabilized in the intersubunit space by dimeric ArfB. Uncovering distinct modes of ArfB function resolves conflicting biochemical and structural studies, and may lead to re-examination of other ribosome rescue pathways, whose functions depend on mRNA lengths.
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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.