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We have isolated a new organic hydroperoxide resistance (ohr ) gene fromXanthomonas campestris pv. phaseoli. This was done by complementation of anEscherichia coli alkyl hydroperoxide reductase mutant with an organic hydroperoxide-hypersensitive phenotype.ohr encodes a 14.5-kDa protein. Its amino acid sequence shows high homology with several proteins of unknown function. Anohr mutant was subsequently constructed, and it showed increased sensitivity to both growth-inhibitory and killing concentrations of organic hydroperoxides but not to either H2 O2 or superoxide generators. No alterations in sensitivity to other oxidants or stresses were observed in the mutant.ohr had interesting expression patterns in response to low concentrations of oxidants. It was highly induced by organic hydroperoxides, weakly induced by H2 O2 , and not induced at all by a superoxide generator. The novel regulation pattern ofohr suggests the existence of a second organic hydroperoxide-inducible system that differs from the global peroxide regulator system, OxyR. Expression ofohr in various bacteria tested conferred increased resistance totert -butyl hydroperoxide killing, but this was not so for wild-typeXanthomonas strains. The organic hydroperoxide hypersensitivity ofohr mutants could be fully complemented by expression ofohr or a combination ofahpC andahpF and could be partially complemented by expressionahpC alone. The data suggested that Ohr was a new type of organic hydroperoxide detoxification protein.

journal of bacteriology

Identification and Characterization of a New Organic Hydroperoxide Resistance ( <i>ohr</i> ) Gene with a Novel Pattern of Oxidative Stress Regulation from <i>Xanthomonas campestris</i> pv. phaseoli