Catalase gene

K20. Kishimoto, Y., Murakami, Y Hayashi, K., Takahara, S., Sugimura, T., and Sekiya, T.. Detection of a common mutation of the catalase gene in Japanese acatalasemic patients. Hum. Genet. 88,487-490(1992). 

The effectors of the mammalian host immune attack against filaria include reactive oxygen intermediates. Filarial nematodes express glutathione peroxidase, thioredoxin peroxidase and superoxide dismutase at their surface - enzymes believed to protect the nematode from this attack (Selkirk et al., 1998). A bacterial catalase gene has been identified that most probably derives from the endosymbiont genome (Henkle-Duhrsen et al., 1998) this enzyme may contribute with other enzymes to the protection of both Wolbachia and its nematode host from oxygen radicals. 

Santanam, N., Auge, N., Zhou, M., Keshava, C., and Parthasarathy, S., 1999, Oveiexpression of human catalase gene decreases oxidized lipid-induced cytotoxicity in vascular smooth muscle cells, Arten osder. Thromb. Vase. Biol. 19 1912-1917. 

Benhamou, P. Y., Moriscot, C., Richard, M. J., Kerr-Conte, J., Pattou, F., Chroboczek, J., Lemarchand, P. and Halimi, S. (1998). Adenoviral-mediated catalase gene transfer protects porcine and human islets in vitro against oxidative stress. Transplant Proc. 30, 459. 

Calera JA, Paris S, Monod M, Hamilton AJ, Debeaupuis JP, Diaquin M, Lopez-Medrano R, Leal F, Latge JP Cloning and dismption of the antigenic catalase gene of Aspergillus fumigatus. Infect Immun 1997 65 2717-2724. 

Lapinskas P, Ruis H, Culotta V. Regulation of Saccharomyces cerevisiae catalase gene expression by copper. Cur Genet 24 388-393, 1993. 

Orr, W. C., and Sohal, R. S., 1992, The effects of catalase gene overexpression on life span and resistance to oxidative stress in transgenic Drosophila melanogaster, Arch. Biochem. Biophys. 297 35-41. 

Halaban, R., and Moellmann, G. (1990). Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity. Proc. Natl. Acad. Sci. USA 87 4809-4813. 

Henkle-Duhrsen, K., Eckelt, V.H., Wildenburg, G., Blaxter, M. and Walter, R.D. (1998) Gene structure, activity and localization of a catalase from intracellular bacteria in Onchocerca volvulus. Molecular and Biochemical Parasitology 96, 69-81. 

Figure 10.8. Proposed model for an Rbo/Rbr oxidative stress protection system in D. vulgaris. Rub, rubredoxin Kat, heme catalase Per, product of the /ar-Iike gene. Reprinted with permission from Lumppio et al. (2001), copyright 2001 American Society for Microbiology.

Some aspects of the proposed Rbr/Rbo oxidative stress defense system in D. vulgaris resemble those recently suggested for oxidative stress protection in the anaerobic hyperthermophilic archaeon Pyrococcus furiosus (Jenney et al. 1999). Pyrococcus furiosus contains an Nlr-like protein with superoxide reductase activity as well as an Rbr, the genes for which are tandemly located. The microorganismic segregation of SOD/catalase between aerobes and anaerobes appears to be less distinct than for Rbo/Rbr, which, as noted above, have so far been found only in air-sensitive microbes (Kirschvink et al. 2000). The latter segregation suggests that the Rbo/Rbr oxidative stress protection system is well suited to protection of anaerobic life in an aerobic world. 

Zou P-J, Borovok I, Ortiz de Orud Lucana D, et al. 1999. The mycelium-associated Streptomyces reticuli catalase-peroxidase, its gene and regulation by FurS. Microbiology 145 549-59. 

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