Induction of the manganese-containing superoxide dismutase in Escherichia coli is independent of the oxidative stress (oxyR-controlled) regulon.
The synthesis of manganese-superoxide dismutase in response to hydrogen peroxide and to paraquat was examined in strains of Escherichia coli with different mutations in the oxyR gene. Hydrogen peroxide treatment did not induce manganese-superoxide dismutase, but did induce the oxyR regulon. Paraquat induced this enzyme in a strain compromised in its ability to induce the defense response against oxidative stress (oxyR deletion) as well as in a strain that is constitutive and overexpresses the oxyR regulon. Catalase (HPI), but not manganese-superoxide dismutase, was over-expressed under anaerobic conditions in a strain harboring a constitutive oxyR mutation. The data clearly demonstrate that the induction of manganese-superoxide dismutase is independent of the oxyR-controlled regulon.
D000693:Anaerobiosis; D002374:Catalase / Q000096:biosynthesis; D004790:Enzyme Induction; D004926:Escherichia coli / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics; D005796:Genes; D005798:Genes, Bacterial; D005809:Genes, Regulator; D005838:Genotype; D006861:Hydrogen Peroxide / Q000494:pharmacology; D008345:Manganese / Q000032:analysis; D009154:Mutation; D010100:Oxygen / Q000494:pharmacology; D010269:Paraquat / Q000494:pharmacology; D013482:Superoxide Dismutase / Q000096:biosynthesis* / Q000235:genetics
D008345:Manganese; D006861:Hydrogen Peroxide; D002374:Catalase; D013482:Superoxide Dismutase; D010269:Paraquat; D010100:Oxygen