ArticleNature chemical biology2020
Dynamics of the context-specific translation arrest by chloramphenicol and linezolid.
Article in Nature chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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Who cites it
35 citing papers in PubMed, 61 citations in OpenAlex.
- Halting translation by the letter with sequence-selective small molecules.Nature chemical biology · 2026Review
- Approaches for Studying Context Specificity of Translation Inhibitor Action.International journal of molecular sciences · 2026Review
- Off-target anti-leukemic effects of antibiotics: mechanisms and therapeutic insights.Cancer chemotherapy and pharmacology · 2026Review
- Antibiotic Mechanisms and Resistance: Molecular Insights and Therapeutic Strategies.Antibiotics (Basel, Switzerland) · 2026Review
- Structural modification of oxazolidinone antibiotics alters nascent peptide stalling preference and peptide trajectory through the ribosome.bioRxiv : the preprint server for biology · 2026Article
- Prodrug florfenicol amine is activated by intrinsic resistance to target Mycobacterium abscessus.Nature microbiology · 2025Article
- 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
- Context-specific inhibition of mitochondrial ribosomes by phenicol and oxazolidinone antibiotics.bioRxiv : the preprint server for biology · 2024Article
- Euglena mutabilis exists in a FAB consortium with microbes that enhance cadmium tolerance.International microbiology : the official journal of the Spanish Society for Microbiology · 2024Article
- Global regulation via modulation of ribosome pausing by the ABC-F protein EttA.Nature communications · 2024Article
- Paenilamicins from the honey bee pathogenbioRxiv : the preprint server for biology · 2024Article
- Central metabolism is a key player in E. coli biofilm stimulation by sub-MIC antibiotics.PLoS genetics · 2023Article
- Bleaching-resistant, Near-continuous Single-molecule Fluorescence and FRET Based on Fluorogenic and Transient DNA Binding.Chemphyschem : a European journal of chemical physics and physical chemistry · 2023Article
- Atlas of mRNA translation and decay for bacteria.Nature microbiology · 2023Article
- Chloramphenicol Derivatization in Its Primary Hydroxyl Group with Basic Amino Acids Leads to New Pharmacophores with High Antimicrobial Activity.Antibiotics (Basel, Switzerland) · 2023Article
- Conjugates of Chloramphenicol Amine and Berberine as Antimicrobial Agents.Antibiotics (Basel, Switzerland) · 2022Article
- Article
- Structural basis for the inability of chloramphenicol to inhibit peptide bond formation in the presence of A-site glycine.Nucleic acids research · 2022Article
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 1 country.
Funding
Abstract
Chloramphenicol (CHL) and linezolid (LZD) are antibiotics that inhibit translation. Both were thought to block peptide-bond formation between all combinations of amino acids. Yet recently, a strong nascent peptide context-dependency of CHL- and LZD-induced translation arrest was discovered. Here we probed the mechanism of action of CHL and LZD by using single-molecule Förster resonance energy transfer spectroscopy to monitor translation arrest induced by antibiotics. The presence of CHL or LZD does not substantially alter dynamics of protein synthesis until the arrest-motif of the nascent peptide is generated. Inhibition of peptide-bond formation compels the fully accommodated A-site transfer RNA to undergo repeated rounds of dissociation and nonproductive rebinding. The glycyl amino-acid moiety on the A-site Gly-tRNA manages to overcome the arrest by CHL. Our results illuminate the mechanism of CHL and LZD action through their interactions with the ribosome, the nascent peptide and the incoming amino acid, perturbing elongation dynamics.
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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.