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J. Biol. Chem., Vol. 266, Issue 14, 8747-8750, May, 1991
SI Liochev and I Fridovich
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.
Effects of overproduction of superoxide dismutase on the toxicity of paraquat toward Escherichia coli
Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710.
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