Effects of overproduction of superoxide dismutase on the toxicity of paraquat toward Escherichia coli.
Gross overproduction of the manganese-containing superoxide dismutase in Escherichia coli, by virtue of a multicopy plasmid bearing the sodA gene, decreases enumeration on paraquat-containing agar plates. This reflects growth inhibition, not lethality, since cells on these plates can be rescued by exclusion of dioxygen. Growth in liquid medium revealed that the control strain adapted to growth in the presence of paraquat more rapidly than did the overproducer. Glucose-6-phosphate dehydrogenase, taken as a representative of the superoxide-inducible soxR regulon, was induced during exposure to paraquat to a much greater extent in the control than in the superoxide dismutase-over-producing strain. These results support the view that overproduction of superoxide dismutase interferes with induction of the soxR regulon and thus prevents a balanced adaptation to the multiple aspects of the toxicity of aerobic paraquat.
Liochev
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SI
Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710.
Fridovich
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D000693:Anaerobiosis; D004790:Enzyme Induction; D004926:Escherichia coli / Q000187:drug effects* / Q000201:enzymology / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial; D005954:Glucosephosphate Dehydrogenase / Q000096:biosynthesis; D006863:Hydrogen-Ion Concentration; D010269:Paraquat / Q000633:toxicity*; D013482:Superoxide Dismutase / Q000235:genetics / Q000378:metabolism*
D005954:Glucosephosphate Dehydrogenase; D013482:Superoxide Dismutase; D010269:Paraquat