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Oxidative stress response in pathogenic mycobacteria is believed to be of significance for host-pathogen interactions at various stages of infection. It also plays a role in determining the intrinsic susceptibility to isoniazid in mycobacterial species. In this work, we characterized theoxyR-ahpC andfurA-katG loci in the nontuberculous pathogenMycobacterium marinum . In contrast toMycobacterium smegmatis and likeMycobacterium tuberculosis andMycobacterium leprae ,M. marinum was shown to possess a closely linked and divergently oriented equivalents of the regulator of peroxide stress responseoxyR and its subordinate geneahpC , encoding a homolog of alkyl hydroperoxide reductase. Purified mycobacterial OxyR was found to bind to theoxyR-ahpC promoter region fromM. marinum and additional mycobacterial species. Mobility shift DNA binding analyses using OxyR binding sites from several mycobacteria and a panel of in vitro-generated mutants validated the proposed consensus mycobacterial recognition sequence.M. marinum AhpC levels detected by immunoblotting, were increased upon treatment with H2 O2 , in keeping with the presence of a functional OxyR and its binding site within the promoter region ofahpC . In contrast, OxyR did not bind to the sequences upstream of thekatG structural gene, andkatG expression did not follow the pattern seen withahpC . Instead, a new open reading frame encoding a homolog of the ferric uptake regulator Fur was identified immediately upstream ofkatG inM. marinum . ThefurA-katG linkage and arrangement are ubiquitous in mycobacteria, suggesting the presence of additional regulators of oxidative stress response and potentially explaining the observed differences inahpC andkatG expression. Collectively, these findings broaden our understanding of oxidative stress response in mycobacteria. They also suggest thatM. marinum will be useful as a model system for studying the role of oxidative stress response in mycobacterial physiology, intracellular survival, and other host-pathogen interactions associated with mycobacterial diseases.

Oxidative Stress Response and Characterization of theoxyR-ahpCandfurA-katGLoci inMycobacterium marinum