Copper/Zinc-Superoxide Dismutase Is Required for Oxytetracycline Resistance of Saccharomyces cerevisiae
| Autor: | Kimberly S. Babb, Srividya Malkapuram, Carolina Mateus, Simon V. Avery |
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| Rok vydání: | 2000 |
| Předmět: |
Transcription
Genetic Mutant Saccharomyces cerevisiae Oxytetracycline Biology Protein oxidation Microbiology Fungal Proteins Superoxide dismutase Lipid peroxidation chemistry.chemical_compound Molecular Biology Protein Synthesis Inhibitors Superoxide Dismutase Tetracycline Resistance Wild type biology.organism_classification Anti-Bacterial Agents Complementation Eukaryotic Cells Biochemistry chemistry Catalase biology.protein Lipid Peroxidation Oxidation-Reduction Gene Deletion |
| Zdroj: | Journal of Bacteriology. 182:76-80 |
| ISSN: | 1098-5530 0021-9193 |
| Popis: | Saccharomyces cerevisiae , along with other eukaryotes, is resistant to tetracyclines. We found that deletion of SOD1 (encoding Cu/Zn superoxide dismutase) rendered S. cerevisiae hypersensitive to oxytetracycline (OTC): a sod1Δ mutant exhibited a >95% reduction in colony-forming ability at an OTC concentration of 20 μg ml −1 , whereas concentrations of up to 1,000 μg ml −1 had no effect on the growth of the wild type. OTC resistance was restored in the sod1 Δ mutant by complementation with wild-type SOD1 . The effect of OTC appeared to be cytotoxic and was not evident in a ctt1 Δ (cytosolic catalase) mutant or in the presence of tetracycline. SOD1 transcription was not induced by OTC, suggesting that constitutive SOD1 expression is sufficient for wild-type OTC resistance. OTC uptake levels in wild-type and sod1 Δ strains were similar. However, lipid peroxidation and protein oxidation were both enhanced during exposure of the sod1 Δ mutant, but not the wild type, to OTC. We propose that Sod1p protects S. cerevisiae against a mode of OTC action that is dependent on oxidative damage. |
| Databáze: | OpenAIRE |
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