ArticleProceedings of the National Academy of Sciences of the United States of America2016
Resistance mutations generate divergent antibiotic susceptibility profiles against translation inhibitors.
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 32 papers.
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Who cites it
32 citing papers in PubMed, 53 citations in OpenAlex.
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- Dual site targeting of the bacterial 70S ribosome by tetracyclines.Nature communications · 2026Article
- Negamycin: Nature's Forgotten Antibiotic.ACS infectious diseases · 2026Review
- Key Proteins and Enzymatic Mechanisms Underlying Drug Resistance in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- T cell toxicity induced by tigecycline binding to the mitochondrial ribosome.Nature communications · 2025Article
- Impacts of ribosomal RNA sequence variation on gene expression and phenotype.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Review
- R3DMCS: a web server for visualizing structural variation in RNA motifs across experimental 3D structures from the same organism or across species.Bioinformatics (Oxford, England) · 2024Article
- Structural basis for differential inhibition of eukaryotic ribosomes by tigecycline.Nature communications · 2024Article
- Bactericidal effect of tetracycline in E. coli strain ED1a may be associated with ribosome dysfunction.Nature communications · 2024Article
- Hibernating ribosomes as drug targets?Frontiers in microbiology · 2024Review
- The structure of a hibernating ribosome in a Lyme disease pathogen.Nature communications · 2023Article
- Structural conservation of antibiotic interaction with ribosomes.Nature structural & molecular biology · 2023Article
- Streptothricin F is a bactericidal antibiotic effective against highly drug-resistant gram-negative bacteria that interacts with the 30S subunit of the 70S ribosome.PLoS biology · 2023Article
- Sarecycline inhibits protein translation in Cutibacterium acnes 70S ribosome using a two-site mechanism.Nucleic acids research · 2023Article
- Article
- Modulating co-translational protein folding by rational design and ribosome engineering.Nature communications · 2022Article
- Studies on Viroid Shed Light on the Role of RNA Three-Dimensional Structural Motifs in RNA Trafficking in Plants.Frontiers in plant science · 2022Review
- Structure of the translatingProceedings of the National Academy of Sciences of the United States of America · 2021Article
- A novel SHAPE reagent enables the analysis of RNA structure in living cells with unprecedented accuracy.Nucleic acids research · 2021Article
- The Antibiotic Negamycin Crosses the Bacterial Cytoplasmic Membrane by Multiple Routes.Antimicrobial agents and chemotherapy · 2021Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
Mutations conferring resistance to translation inhibitors often alter the structure of rRNA. Reduced susceptibility to distinct structural antibiotic classes may, therefore, emerge when a common ribosomal binding site is perturbed, which significantly reduces the clinical utility of these agents. The translation inhibitors negamycin and tetracycline interfere with tRNA binding to the aminoacyl-tRNA site on the small 30S ribosomal subunit. However, two negamycin resistance mutations display unexpected differential antibiotic susceptibility profiles. Mutant U1060A in 16S Escherichia coli rRNA is resistant to both antibiotics, whereas mutant U1052G is simultaneously resistant to negamycin and hypersusceptible to tetracycline. Using a combination of microbiological, biochemical, single-molecule fluorescence transfer experiments, and X-ray crystallography, we define the specific structural defects in the U1052G mutant 70S E. coli ribosome that explain its divergent negamycin and tetracycline susceptibility profiles. Unexpectedly, the U1052G mutant ribosome possesses a second tetracycline binding site that correlates with its hypersusceptibility. The creation of a previously unidentified antibiotic binding site raises the prospect of identifying similar phenomena in antibiotic-resistant pathogens in the future.
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