ArticleProceedings of the National Academy of Sciences of the United States of America2017
Miscoding-induced stalling of substrate translocation on the bacterial ribosome.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 34 citations in OpenAlex.
- Near-cognate tRNAs enhance tRNA rejection and prime the ribosome for rapid subsequent tRNA testing.Biophysical journal · 2025Article
- Kinetic mechanism and determinants of EF-P recruitment to translating ribosomes.Nucleic acids research · 2024Article
- Single-Molecule Studies of Cognate and Near-Cognate Elongation in anbioRxiv : the preprint server for biology · 2024Article
- Alternate conformational trajectories in ribosome translocation.PLoS computational biology · 2024Article
- β-Amino Acids Reduce Ternary Complex Stability and Alter the Translation Elongation Mechanism.ACS central science · 2024Article
- β-amino acids reduce ternary complex stability and alter the translation elongation mechanism.bioRxiv : the preprint server for biology · 2024Article
- Insights into translocation mechanism and ribosome evolution from cryo-EM structures of translocation intermediates of Giardia intestinalis.Nucleic acids research · 2023Article
- Hyper-swivel head domain motions are required for complete mRNA-tRNA translocation and ribosome resetting.Nucleic acids research · 2022Article
- Diffusion control in biochemical specificity.Biophysical journal · 2022Article
- Drop-off-reinitiation triggered by EF-G-driven mistranslocation and its alleviation by EF-P.Nucleic acids research · 2022Article
- Optimization of a fluorescent-mRNA based real-time assay for precise kinetic measurements of ribosomal translocation.RNA biology · 2021Article
- Mechanistic insights into translation inhibition by aminoglycoside antibiotic arbekacin.Nucleic acids research · 2021Article
- Article
- Translation error clusters induced by aminoglycoside antibiotics.Nature communications · 2021Article
- Ataluren and aminoglycosides stimulate read-through of nonsense codons by orthogonal mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Translational regulation of environmental adaptation in bacteria.The Journal of biological chemistry · 2020Review
- NMR and crystallographic structural studies of the Elongation factor P from Staphylococcus aureus.European biophysics journal : EBJ · 2020Article
- Dynamics of the context-specific translation arrest by chloramphenicol and linezolid.Nature chemical biology · 2020Article
- Approaches for measuring the dynamics of RNA-protein interactions.Wiley interdisciplinary reviews. RNA · 2020Review
- A single H/ACA small nucleolar RNA mediates tumor suppression downstream of oncogenic RAS.eLife · 2019Article
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2 authors at 2 institutions in 1 country.
Funding
Abstract
Directional transit of the ribosome along the messenger RNA (mRNA) template is a key determinant of the rate and processivity of protein synthesis. Imaging of the multistep translocation mechanism using single-molecule FRET has led to the hypothesis that substrate movements relative to the ribosome resolve through relatively long-lived late intermediates wherein peptidyl-tRNA enters the P site of the small ribosomal subunit via reversible, swivel-like motions of the small subunit head domain within the elongation factor G (GDP)-bound ribosome complex. Consistent with translocation being rate-limited by recognition and productive engagement of peptidyl-tRNA within the P site, we now show that base-pairing mismatches between the peptidyl-tRNA anticodon and the mRNA codon dramatically delay this rate-limiting, intramolecular process. This unexpected relationship between aminoacyl-tRNA decoding and translocation suggests that miscoding antibiotics may impact protein synthesis by impairing the recognition of peptidyl-tRNA in the small subunit P site during EF-G-catalyzed translocation. Strikingly, we show that elongation factor P (EF-P), traditionally known to alleviate ribosome stalling at polyproline motifs, can efficiently rescue translocation defects arising from miscoding. These findings help reveal the nature and origin of the rate-limiting steps in substrate translocation on the bacterial ribosome and indicate that EF-P can aid in resuming translation elongation stalled by miscoding errors.
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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.