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. 1992 Nov;138(11):2363-70.
doi: 10.1099/00221287-138-11-2363.

The catalase-peroxidase of Mycobacterium intracellulare: nucleotide sequence analysis and expression in Escherichia coli

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The catalase-peroxidase of Mycobacterium intracellulare: nucleotide sequence analysis and expression in Escherichia coli

S L Morris et al. J Gen Microbiol. 1992 Nov.

Abstract

The activation of catalase genes in response to oxidative stress may contribute to the intracellular survival of mycobacteria. In this report, the nucleotide sequence of a mycobacterial catalase gene is described. The deduced protein sequence of this Mycobacterium intracellulare gene (MI85) was 60% identical to the Escherichia coli hydroperoxidase I (HPI) protein, 59% identical to the Salmonella typhimurium (HPI) catalase, and 47% identical to a Bacillus stearothermophilus peroxidase. The MI85 protein, expressed in E. coli, has also been shown to have peroxidase and catalase activities. Furthermore, Southern blot hybridizations, which demonstrated that a MI85 gene probe hybridizes with chromosomal DNA from thirteen different strains of mycobacteria, suggest that this catalase-peroxidase gene is prevalent in the mycobacterial genus. The availability of catalase gene probes should permit an evaluation, at the molecular level, of the role of catalase in mycobacterial pathogenesis.

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