Production of catalases by Comamonas spp. and resistance to oxidative stress

Folia Microbiologica

Volumn 50, Issue 2, 2005, Pages 113-118

  Godocikova J ^a   Bohacova V ^a   Zamocky M ^a   Polek, B ^a  

^a INSTITUTE OF CHEMISTRY   (Slovakia)

Author keywords

[No Author keywords available]

Indexed keywords

COMAMONAS; COMAMONAS TERRIGENA; COMAMONAS TESTOSTERONI;

EID: 22844438569     PISSN: 00155632     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02931458     Document Type: Article

References (33)

1. ANDERSON A.J., MILLER C.D.: Catalase activity and the survival of Pseudomonas putida, a root colonizer, upon treatment with peracetic acid. Can.J.Microbiol. 47, 222-228 (2001).
2. BAE H.S., LEE J.M., KIM Y.B., LEE S.T.: Biodegradation of the mixture of 4-chlorophenol and phenol by Comamonas testosteroni CPW301. Biodegradation 7, 463-469 (1996).
3. BARKAY T., PRITCHARD H.: Adaptation of aquatic microbial communities to pollutant stress. Microbiol.Sci. 5, 165-169 (1988).
4. BISHAI W.R., HOWARD N.S., WINKELSTEIN J.A., SMITH H.O.: Characterization and virulence analysis of catalase mutants of Haemophilus influenzae. Infect.Immun. 62, 4855-4860 (1994).
5. BRADFORD M.M.: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal.Biochem. 72, 248-250 (1976).
6. DOWDS B.C.: The oxidative stress response in Bacillus subtilis. FEMS Microbiol.Lett. 124, 255-263 (1994).
7. DOWDS B.C.A., MURPHY P., MCCONNELL D.J., DEVINE K.M.: Relationship among oxidative stress, growth cycle, and sporulation in Bacillus subtilis. J.Bacteriol. 169, 5771-5775 (1987).
8. FERIANC P., POLEK B., GODOČÍKOVÁ J., TÓTH D.: Metabolic activity of cadmium-stressed and/or starved Vibrio sp. Folia Microbiol. 40, 443-446 (1995).
9. GILLE G., SIGLER K.: Oxidative stress and living cells. Folia Microbiol. 40, 131-152 (1995).
10. GODOČÍKOVÁ J., POLEK B., WHITE G.F., FERIANC P., TOTH D.: Dioctyl sulphosuccinate utilization and mineralization by bacteria Comamonas terrigena N3H. Biologia 52, 741-745 (1997).
11. 14C]succinate in relation to adaptation of bacterium, Comamonas terrigena, to dialkyl esters of sulphosuccinate. Biotechnol.Lett. 26, 1497-1500 (2004).
12. HALLIWELL B., GUTTERIDGE M.C.: Free Radicals in Biology and Medicine, pp. 105-350. Oxford University Press, Oxford 1999.
13. 2 challenge in Escherichia coli. J.Bacteriol. 170, 3910-3914 (1988).
14. KAPPUS H.: Oxidative stress in chemical toxicity. Arch.Toxicol. 60, 144-149 (1987).
15. LOPRASERT S., VATTANAVIBOON P., PRAITUAN W., CHAMNONGPOL S., MONGKOLSUK S.: Regulation of the oxidative stress protective enzymes, catalase and superoxide dismutase in Xanthomonas - a review. Gene 179, 33-37 (1996).
16. MULEY M.R., SWITALA J., BORYS A., LOEWEN P.C.: Regulation of transcription of katF in Escherichia coli. J.Bacteriol. 172, 6713-6720 (1990).
17. MURPHY P., DOWDS B.C.A., MCCONNEL D.J., DEVINE K.M.: Oxidative stress and growth temperature in Bacillus subtilis. J.Bacteriol. 169, 5766-5770 (1987).
18. ODENBREIT S., WIELAND B., HAAS R.: Cloning and genetic characterization of Helicobacter pylori catalase and construction of a catalase-deficient mutant strain. J.Bacteriol. 178, 6960-6967 (1996).
19. PARK Y.B., HAN Y.H.: Increased activities of SOD and catalases on aerobic growth in Arcobacter nitrofigilis. J.Microbiol. 35, 239-240 (1997).
20. PETERS M., HEINARU A., NURK A.: Plasmid-encoded catalase KatA, the main catalase of Pseudomonas fluorescens strain Cb36. FEMS Microbiol.Lett. 200, 235-240 (2000).
21. PROKŠOVÁ M., AUGUSTÍN J., VRBANOVÁ A.: Enrichment, isolation and characterization of dialkyl sulfosuccinate degrading bacteria Comamonas terrigena N3H and Comamonas terrigena NIC. Folia Microbiol. 42, 635-639 (1997).
22. ROGGENKAMP R., SAHM H., WAGNER F.: Microbial assimilation of methanol induction and function of catalase in Candida boidinii. FEBS Lett. 41, 283-286 (1974).
23. SHA Z., STABEL T.J., MAYFIELD J.E.: Brucella abortus catalase is a periplasmic protein lacking a standard signal sequence. J.Bacteriol. 176, 7375-7377 (1994).
24. VATTANAVIBOON P., MONGKOLSUK S.: Unusual adaptive, cross protection responses and growth phase resistance against peroxide killing in a bacterial shrimp pathogen, Vibrio harveyi. FEMS Microbiol.Lett. 200, 111-116 (2001).
25. VATTANAVIBOON P., WHANGSUK W., MONGKOLSUK S.: A suppressor of the menadione-hypersensitive phenotype of a Xanthomonas campestris pv. phaseoli oxyR mutant reveals a novel mechanism of toxicity and the protective role of alkyl hydroperoxide reductase. J.Bacteriol. 185, 1743-1748 (2003).
26. WINQUIST L., RANNUNG U., RANNUNG A., RAMEL C.: Protection from toxic and mutagenic effects of hydrogen peroxide by catalase induction in Salmonella typhimurium. Mutat.Res. 141, 145-147 (1984).
27. WOODBURY W.A., SPENCER K., STAHLMANN M.A.: An improved procedure using ferricyanide for detecting catalase isozymes. Anal.Biochem. 44, 301-305 (1971).
28. YUMOTO I., IWATA H., SAWABE T., VENO K., ICHISE N., MATSUJAMA H., OKUYAMA H., KAWASAKI K.: Characterization of facultatively psychrophilic bacterium Vibrio rumoiensis sp.nov., that exhibits high catalase activity. Appl.Environ.Microbiol. 65, 67-72 (1999).
29. YUN E.J., LEE Y.N.: Production of two different catalase-peroxidases by Deinococcus radiophilus. FEMS Microbiol.Lett. 184, 155-159 (2000).
30. ZÁMOCKÝ M., HERZOG C., NYKYRI L.M., KOLLER F.: Site-directed mutagenesis of the lower parts of yeast catalase A leads to highly increased peroxidatic activity. FEBS Lett. 367, 241-245 (1995).
31. ZÁMOCKÝ M., GODOČÍKOVÁ J., KOLLER F., POLEK B.: Potential application of catalase-peroxidase from Comamonas terrigena N3H in the biodegradation of phenolic compounds. Antonie van Leeuwenhoek 79, 109-117 (2001).
32. ZÁMOCKÝ M., POLEK B., GODOČÍKOVÁ J., KOLLER F.: Oxidative stress-induced expression of catalases in Comamonas terrigena. Folia Microbiol. 47, 235-240 (2002).
33. ZÁMOCKÝ M., GODOČÍKOVÁ J., GAŠPERÍK J., KOLLER F., POLEK B.: Expression, purification, and sequence analysis of catalase-1 from the soil bacterium Comamonas terrigena N3H. Protein Expres.Purif. 36, 115-123 (2004).