Catalase-peroxidase of Caulobacter crescentus: Function and role in stationary-phase survival

Journal of Bacteriology

Volumn 179, Issue 21, 1997, Pages 6831-6836

  Steinman, Howard M ^a   Fareed, Fareed ^a   Weinstein, Laurie ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; HYDROGEN PEROXIDE; PEROXIDASE;

ARTICLE; BACTERIAL GROWTH; CAULOBACTER CRESCENTUS; CELL SURVIVAL; ENZYME ACTIVITY; ENZYME ASSAY; ESCHERICHIA COLI; GROWTH RATE; NONHUMAN; OXIDATIVE STRESS; PHENOTYPE; PRIORITY JOURNAL; STARVATION;

BACTERIA (MICROORGANISMS); CAULOBACTER VIBRIOIDES; ESCHERICHIA COLI;

EID: 0030693196     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.21.6831-6836.1997     Document Type: Article

References (35)

1. Aebi, H. 1984. Catalase in vitro. Methods Enzymol. 108:121-126.
2. Allen, H. L. 1971. Primary productivity, chemoorganotrophy, and nutritional interactions of epiphytic algae and bacteria on macrophytes in the littoral of a lake. Ecol. Monogr. 41:97-127.
3. Alley, M. R. K., S. L. Gomes, W. Alexander, and L. Shapiro. 1991. Genetic analysis of a temporally transcribed chemotaxis gene cluster in Caulobacter crescentus. Genetics 129:333-342.
4. Ausubel, F. M., R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.). 1994. Current protocols in molecular biology. John Wiley & Sons, Inc., New York, N.Y.
5. Claiborne, A., and I. Fridovich. 1979. Purification of the o-dianisidine peroxidase from Escherichia coli B. Physicochemical characterization and analysis of its dual catalatic and peroxidatic activities. J. Biol. Chem. 254:4245-4252.
6. Colombi, D., and S. L. Gomes. 1997. An alkB gene homolog is differentially transcribed during the Caulobacter crescentus cell cycle. J. Bacteriol. 179: 3139-3145.
7. Demple, B., and J. Halbrook. 1983. Inducible repair of oxidative DNA damage in Escherichia coli. Nature 304:466-468.
8. Ely, B. 1991. Genetics of Caulobacter crescentus. Methods Enzymol. 204:372-384.
9. Evinger, M., and N. Agabian. 1977. Envelope-associated nucleoid from Caulobacter crescentus stalked and swarmer cells. J. Bacteriol. 132:294-301.
10. 9a.Gonzalez-Flecha, B., and B. Demple. 1995. Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli. J. Biol. Chem. 270:13681-13687.
11. Gonzalez-Flecha, B., and B. Demple. 1997. Homeostatic regulation of intracellular hydrogen peroxide concentration in aerobically growing Escherichia coli. J. Bacteriol. 179:382-388.
12. Hochman, A., A. Figueredo, and J. D. Wall. 1991. Physiological functions of hydroperoxidases in Rhodobacter capsulatus. J. Bacteriol. 174:3386-3391.
13. Huisman, G. W., D. A. Siegele, M. A. Zamgrano, and R. Kolter. 1996. Morphological and physiological changes during stationary phase, p. 1672-1682. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. American Society for Microbiology, Washington, D.C.
14. 2 challenge in Escherichia coli. J. Bacteriol. 170:3910-3914.
15. Johnson, R. C., and B. Ely. 1977. Isolation of spontaneously derived mutants of Caulobacter crescentus. Genetics 86:25-32.
16. Lapteva, N. A. 1987. Ecological features of distribution of bacteria of the genus Caulobacter in freshwater bodies. Mikrobiologiya 56:537-543.
17. Loewen, P. C. 1984. Isolation of catalase-deficient Escherichia coli mutants and genetic mapping of katE, a locus that affects catalase activity. J. Bacteriol. 157:622-626.
18. Marcinkeviciene, J. A., R. S. Magliozzo, and J. S. Blanchard. 1996. Purification and characterization of the Mycobacterium smegmatis catalase-peroxidase involved in isoniazid activation. J. Biol. Chem. 270:22290-22295.
19. Miller, J. H. 1992. A short course in bacterial genetics. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
20. Mohr, C. D., U. Jenal, and L. Shapiro. 1996. Flagellar assembly in Caulobacter crescentus: a basal body P-ring null mutation affects stability of the L-ring protein. J. Bacteriol. 178:675-682.
21. Mulvey, M. R., J. Switala, A. Borys, and P. C. Loewen. 1990. Regulation of transcription of katE and katF in Escherichia coli. J. Bacteriol. 172:6713-6720.
22. Poindexter, J. S. 1964. Biological properties and classification of the Caulobacter group. Bacteriol. Rev. 28:231-295.
23. Poindexter, J. S. 1981. The caulobacters: ubiquitous unusual bacteria. Microbiol. Rev. 45:123-179.
24. Prentki, P., and H. M. Krisch. 1984. In vitro insertional mutagenesis with a selectable DNA fragment. Gene 20:303-3133.
25. 32 homolog in Caulobacter crescentus. J. Bacteriol. 178:1919-1927.
26. Schellhorn, H. E., and V. L. Stones. 1992. Regulation of katF and katE in Escherichia coli K-12 by weak acids. J. Bacteriol. 174:4769-4776.
27. Schnell, S., and H. M. Steinman. 1995. Function and stationary-phase induction of periplasmic copper-zinc superoxide dismutase and catalase/peroxidase in Caulobacter crescentus. J. Bacteriol. 177:5924-5929.
28. Shapiro, L., and R. Losick. 1997. Protein localization and cell fate in bacteria. Science 276:712-718.
29. Steinman, H. M. 1985. Bacteriocuprein superoxide dismutases in pseudomonads. J. Bacteriol. 162:1255-1260.
30. Steinman, H. M., and B. Ely. 1990. Copper-zinc superoxide dismutase of Caulobacter crescentus: cloning, sequencing, and mapping of the gene and periplasmic location of the enzyme. J. Bacteriol. 172:2901-2910.
31. St. John, G., and H. M. Steinman. 1996. Periplasmic copper-zinc superoxide dismutase of Legionella pneumophila. A role in stationary phase survival. J. Bacteriol. 178:1578-1584.
32. Storz, G., and S. Altuvia. 1994. OxyR regulon. Methods Enzymol. 234:217-223.
33. Triggs-Raine, B. L., B. W. Doble, M. R. Mulvey, P. A. Sorby, and P. C. Loewen. 1988. Nucleotide sequence of katG, encoding catalase HPI of Escherichia coli. J. Bacteriol. 170:4415-4419.
34. von Ossowski, I., M. R. Mulvey, P. A. Leco, A. Borys, and P. C. Loewen. 1991. Nucleotide sequence of Escherichia coli katE, which encodes catalase HpII. J. Bacteriol. 173:514-520.
35. Welinder, K. G. 1991. Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily. Biochim. Biophys. Acta 1080: 215-220.