ArticleProceedings of the National Academy of Sciences of the United States of America2016
Context-specific inhibition of translation by ribosomal antibiotics targeting the peptidyl transferase center.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.
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Who cites it
103 citing papers in PubMed, 167 citations in OpenAlex.
- Antimicrobial Resistance in Major Gram-Positive Pathogens: Beyond the Vancomycin Border.Antibiotics (Basel, Switzerland) · 2026Review
- Approaches for Studying Context Specificity of Translation Inhibitor Action.International journal of molecular sciences · 2026Review
- Article
- Translation Inhibiting Antibiotics Induce an asRNA Regulating Purine Metabolism inbioRxiv : the preprint server for biology · 2026Article
- Dual site targeting of the bacterial 70S ribosome by tetracyclines.Nature communications · 2026Article
- iTP-seq: a scalable profiling workflow to characterize bacterial translation landscapes in vitro.Nature protocols · 2026Review
- Antibiotic Mechanisms and Resistance: Molecular Insights and Therapeutic Strategies.Antibiotics (Basel, Switzerland) · 2026Review
- A streamlined, nanopore-compatible 5PSeq protocol for rapid phenotypic antimicrobial sensitivity testing.Cell reports methods · 2026Article
- Context-dependent translation inhibition as a cancer therapeutic modality.Nature communications · 2026Article
- Structural modification of oxazolidinone antibiotics alters nascent peptide stalling preference and peptide trajectory through the ribosome.bioRxiv : the preprint server for biology · 2026Article
- How tailored Ribo-seq methods probe unique translation events.RNA (New York, N.Y.) · 2026Review
- Article
- Natural products influence bacteriophage infectivity.Natural product reports · 2025Review
- Structural insights into context-specific inhibition of bacterial translation by macrolides.Nature communications · 2025Article
- The stringent response does not influence ribosome pausing in Bacillus subtilis.Nucleic acids research · 2025Article
- Article
- Structural insights into context-dependent inhibitory mechanisms of chloramphenicol in cells.Nature structural & molecular biology · 2025Article
- Context-specific inhibition of mitochondrial ribosomes by phenicol and oxazolidinone antibiotics.Nucleic acids research · 2025Article
- Paenilamicins are context-specific translocation inhibitors of protein synthesis.Nature chemical biology · 2024Article
- Berberine analog of chloramphenicol exhibits a distinct mode of action and unveils ribosome plasticity.Structure (London, England : 1993) · 2024Article
43 more citing papers are in PubMed but not listed here.
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8 authors at 1 institution in 1 country.
Funding
Abstract
The first broad-spectrum antibiotic chloramphenicol and one of the newest clinically important antibacterials, linezolid, inhibit protein synthesis by targeting the peptidyl transferase center of the bacterial ribosome. Because antibiotic binding should prevent the placement of aminoacyl-tRNA in the catalytic site, it is commonly assumed that these drugs are universal inhibitors of peptidyl transfer and should readily block the formation of every peptide bond. However, our in vitro experiments showed that chloramphenicol and linezolid stall ribosomes at specific mRNA locations. Treatment of bacterial cells with high concentrations of these antibiotics leads to preferential arrest of translation at defined sites, resulting in redistribution of the ribosomes on mRNA. Antibiotic-mediated inhibition of protein synthesis is most efficient when the nascent peptide in the ribosome carries an alanine residue and, to a lesser extent, serine or threonine in its penultimate position. In contrast, the inhibitory action of the drugs is counteracted by glycine when it is either at the nascent-chain C terminus or at the incoming aminoacyl-tRNA. The context-specific action of chloramphenicol illuminates the operation of the mechanism of inducible resistance that relies on programmed drug-induced translation arrest. In addition, our findings expose the functional interplay between the nascent chain and the peptidyl transferase center.
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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.