scholarly journals The complete amino acid sequence of copper, zinc superoxide dismutase from Saccharomyces cerevisiae

1979 ◽  
Vol 44 (4) ◽  
pp. 201-217 ◽  
Author(s):  
Jack T. Johansen ◽  
Carsten Overballe-Petersen ◽  
Brian Martin ◽  
Villy Hasemann ◽  
Ib Svendsen
1995 ◽  
Vol 270 (50) ◽  
pp. 29991-29997 ◽  
Author(s):  
Valeria Cizewski Culotta ◽  
Hung-Dong Joh ◽  
Su-Ju Lin ◽  
Kimberly Hudak Slekar ◽  
Jeffrey Strain

2000 ◽  
Vol 182 (1) ◽  
pp. 76-80 ◽  
Author(s):  
Simon V. Avery ◽  
Srividya Malkapuram ◽  
Carolina Mateus ◽  
Kimberly S. Babb

ABSTRACT Saccharomyces cerevisiae, along with other eukaryotes, is resistant to tetracyclines. We found that deletion ofSOD1 (encoding Cu/Zn superoxide dismutase) renderedS. cerevisiae hypersensitive to oxytetracycline (OTC): asod1Δ 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 sod1Δ mutant by complementation with wild-type SOD1. The effect of OTC appeared to be cytotoxic and was not evident in a ctt1Δ (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 sod1Δ strains were similar. However, lipid peroxidation and protein oxidation were both enhanced during exposure of the sod1Δ 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.


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