ArticleNature chemical biology2020
Tetracenomycin X inhibits translation by binding within the ribosomal exit tunnel.
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 55 papers.
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Who cites it
55 citing papers in PubMed, 79 citations in OpenAlex.
- Structure-based design and synthesis of group A streptogramins that bind to the nascent peptide exit tunnel of the ribosome.European journal of medicinal chemistry · 2026Article
- Halting translation by the letter with sequence-selective small molecules.Nature chemical biology · 2026Review
- The Oxytetracycline ProducerInternational journal of molecular sciences · 2026Article
- Approaches for Studying Context Specificity of Translation Inhibitor Action.International journal of molecular sciences · 2026Review
- Atypical Tetracyclines Promote Longevity and Ferroptotic Neuroprotection via Translation Attenuation.Aging cell · 2026Article
- Cryo-EM reveals multiple mechanisms of ribosome inhibition by doxycycline.Nature communications · 2026Article
- Dual site targeting of the bacterial 70S ribosome by tetracyclines.Nature communications · 2026Article
- Benzoxaborole-modified azithromycins inhibit translation without inducingAntimicrobial agents and chemotherapy · 2026Article
- Atypical tetracyclines promote longevity and ferroptotic neuroprotection via translation attenuation.bioRxiv : the preprint server for biology · 2026Article
- Regioselective approach to 5-arylsulfonylisoxazoles and their antimicrobial activity.Beilstein journal of organic chemistry · 2026Article
- Characterization ofInternational journal of molecular sciences · 2025Article
- The p48 isoform of the PA2G4/EBP1/ITAF45 oncoprotein is required for the encephalomyocarditis virus IRES-driven translation initiation.Nucleic acids research · 2025Article
- Tetracenomycin Aglycones Primarily Inhibit Cell Growth and Proliferation in Mammalian Cancer Cell Lines.Applied sciences (Basel, Switzerland) · 2025Article
- Structural basis of enhanced stalling efficiency of an engineered ribosome arrest peptide.Nucleic acids research · 2025Article
- Diverse chemotypes of polyketides as promising antimicrobial agents: latest progress.RSC advances · 2025Review
- T cell toxicity induced by tigecycline binding to the mitochondrial ribosome.Nature communications · 2025Article
- Visualizing the modification landscape of the human 60S ribosomal subunit at close to atomic resolution.Nucleic acids research · 2025Article
- Genomic and Phenotypic Characterization ofMicroorganisms · 2024Article
- Macrolones target bacterial ribosomes and DNA gyrase and can evade resistance mechanisms.Nature chemical biology · 2024Article
- Paenilamicins are context-specific translocation inhibitors of protein synthesis.Nature chemical biology · 2024Article
Corrections and comments
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Authors and funding
24 authors at 6 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The increase in multi-drug resistant pathogenic bacteria is making our current arsenal of clinically used antibiotics obsolete, highlighting the urgent need for new lead compounds with distinct target binding sites to avoid cross-resistance. Here we report that the aromatic polyketide antibiotic tetracenomycin (TcmX) is a potent inhibitor of protein synthesis, and does not induce DNA damage as previously thought. Despite the structural similarity to the well-known translation inhibitor tetracycline, we show that TcmX does not interact with the small ribosomal subunit, but rather binds to the large subunit, within the polypeptide exit tunnel. This previously unappreciated binding site is located adjacent to the macrolide-binding site, where TcmX stacks on the noncanonical basepair formed by U1782 and U2586 of the 23S ribosomal RNA. Although the binding site is distinct from the macrolide antibiotics, our results indicate that like macrolides, TcmX allows translation of short oligopeptides before further translation is blocked.
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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.