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A gene encoding catalase (hydrogen-peroxide:hydrogen-peroxide oxidoreductase; EC 1.11.1.6) from Campylobacter jejuni was cloned by functional complementation of a catalase-deficient mutant of Escherichia coli. The catalase structural gene, designated katA, was assigned by subcloning and its nucleotide sequence determined. The deduced protein product of 508 amino acids, which had a calculated molecular mass of 58,346 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 Campylobacter coli via natural transformation. Genetic and enzymic analyses of a tetracycline-resistant C. coli 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 H2O2.

microbiology

Molecular characterization of katA from Campylobacter jejuni and generation of a catalase-deficient mutant of Campylobacter coli by interspecific allelic exchange