A gene encoding catalase (hydrogen-peroxide: hydrogen-peroxide oxidoreductase; EC from was cloned by functional complementation of a catalase-deficient mutant of . The catalase structural gene, designated , was assigned by subcloning and its nucleotide sequence determined. The deduced protein product of 508 amino acids, which had a calculated molecular mass of 58346 Da, was found to be structurally and enzymically similar to hydrogen-peroxidases from other bacterial species. The region of DNA containing the structural catalase gene was disrupted by insertion of a tetracycline-resistance marker and the modified sequence then introduced into a strain of via natural transformation. Genetic and enzymic analyses of a tetracycline-resistant transformant confirmed that catalase-deficient mutants had arisen via interspecific allelic exchange. Compared to the isogenic parental strain the mutant was more sensitive to killing by HO.


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