ArticleAntimicrobial agents and chemotherapy2014
Structural analysis of base substitutions in Thermus thermophilus 16S rRNA conferring streptomycin resistance.
Article in Antimicrobial agents and chemotherapy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Acquisition of Streptomycin Resistance by Oxidative Stress Induced by Hydrogen Peroxide in Radiation-Resistant BacteriumInternational journal of molecular sciences · 2022Article
- RsmG forms stable complexes with premature small subunit rRNA during bacterial ribosome biogenesis.RSC advances · 2020Article
- Antibiotic Susceptibility Profiles of Lactic Acid Bacteria from the Human Vagina and Genetic Basis of Acquired Resistances.International journal of molecular sciences · 2020Article
- Aminoglycoside ribosome interactions reveal novel conformational states at ambient temperature.Nucleic acids research · 2018Article
- Resistance to UV Irradiation Caused by Inactivation ofJournal of bacteriology · 2018Article
- Structural landscape of base pairs containing post-transcriptional modifications in RNA.RNA (New York, N.Y.) · 2017Article
- Antibiotic Resistance-Susceptibility Profiles ofFrontiers in microbiology · 2017Article
- Resistance mutations generate divergent antibiotic susceptibility profiles against translation inhibitors.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Streptomycin is a bactericidal antibiotic that induces translational errors. It binds to the 30S ribosomal subunit, interacting with ribosomal protein S12 and with 16S rRNA through contacts with the phosphodiester backbone. To explore the structural basis for streptomycin resistance, we determined the X-ray crystal structures of 30S ribosomal subunits from six streptomycin-resistant mutants of Thermus thermophilus both in the apo form and in complex with streptomycin. Base substitutions at highly conserved residues in the central pseudoknot of 16S rRNA produce novel hydrogen-bonding and base-stacking interactions. These rearrangements in secondary structure produce only minor adjustments in the three-dimensional fold of the pseudoknot. These results illustrate how antibiotic resistance can occur as a result of small changes in binding site conformation.
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