Stable form of ascorbate peroxidase from the red alga galdieria partita similar to both chloroplastic and cytosolic isoforms of higher plants

Bioscience, Biotechnology and Biochemistry

Volumn 66, Issue 11, 2002, Pages 2367-2375

  Kitajima, Sakihito ^a,d   Ueda, Masami ^a   Sano, Satoshi ^a,e   Miyake, Chikahiro ^b,f   Kohchi, Takayuki ^b   Tomizawa, Ken Ichi ^a   Shigeoka, Shigeru ^c   Yokota, Akiho ^a  

^a RESEARCH INSTITUTE OF INNOVATIVE TECHNOLOGY FOR THE EARTH   (Japan)

^b NARA INSTITUTE OF SCIENCE AND TECHNOLOGY   (Japan)

^c KINKI UNIVERSITY   (Japan)

^d KYOTO INSTITUTE OF TECHNOLOGY   (Japan)

^e KYOTO PREFECTURAL UNIVERSITY   (Japan)

^f KYUSHU UNIVERSITY   (Japan)

Author keywords

Cdna; Inactivation; Reactive oxygen species; Recombinant protein

Indexed keywords

ASCORBATE PEROXIDASE; ASCORBIC ACID; COMPLEMENTARY DNA; DRUG DERIVATIVE; ISOENZYME; PEROXIDASE; RECOMBINANT PROTEIN; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CHLOROPLAST; CYTOSOL; ENZYME STABILITY; ENZYMOLOGY; GENETICS; GREEN ALGA; IMMUNOBLOTTING; KINETICS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PLANT; RED ALGA; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; SPECTROPHOTOMETRY;

ALGAE, GREEN; ALGAE, RED; AMINO ACID SEQUENCE; ASCORBIC ACID; BASE SEQUENCE; CHLOROPLASTS; CYTOSOL; DNA, COMPLEMENTARY; ENZYME STABILITY; IMMUNOBLOTTING; ISOENZYMES; KINETICS; MOLECULAR SEQUENCE DATA; PEROXIDASES; PLANT PROTEINS; PLANTS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SPECTROPHOTOMETRY;

ALGAE; EMBRYOPHYTA; ESCHERICHIA COLI; EUKARYOTA; GALDIERIA; GALDIERIA PARTITA; RHODOPHYTA;

EID: 0042536222     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.66.2367     Document Type: Article

References (35)

1. Asada, K., Production and action of active oxygen species in photosynthetic tissues. In “Causes of Pho-tooxidative Stress and Amelioration of Defense Systems in Plants”, eds. Foyer, C. H., and Mullineaux, P. M., CRC press, Boca Raton, pp. 77-107 (1994).
2. Asada, K., The water-water cycle in chloroplasts: scavenging of active oxygens and dissipation of excess photons. Annu. Rev. Plant Physiol. Plant Mol. Biol., 50, 601-639 (1999).
3. Welinder, K. G., Superfamily of plant, fungal and bacterial peroxidase. Curr. Opin. Struc. Biol., 2, 388-393 (1992).
4. Patterson, W. R., Poulos, T. L., and Goodin, D. B., Identification of a porphyrin p cation radical in ascor-bate peroxidase compound I. Biochemistry, 34, 4342-4345 (1995).
5. Patterson, W. R., and Poulos, T. L., Crystal structure of recombinant Pea cytosolic ascorbate peroxidase. Biochemistry, 34, 4331-4341 (1995).
6. Hill, A. P., Modi, S., Sutcliffe, M. J., Turner, D. D., Gilfoyle, D. J., Smith, A. T., Tam, B. M., and Lloyd, E., Chemical, spectroscopic and structural investigation of the substrate-binding site in ascorbate peroxidase. Eur. J. Biochem., 248, 347-354 (1997).
7. Shigeoka, S., Ishikawa, T., Tamoi, M., Miyagawa, Y., Yabuta, Y., and Yoshimura, K., Regulation and function of ascorbate peroxidase isozymes. J. Exp. Bot., 53, 1305-1319 (2002).
8. Miyake, C., and Asada, K., Inactivation mechanism of ascorbate peroxidase at low concentrations of ascorbate: hydrogen peroxide decomposes compound I of ascorbate peroxidase. Plant Cell Physiol., 37, 423-430 (1996).
9. Asada, K., and Kiso, K., Initiation of aerobic oxidation of sulfite by illuminated spinach chloroplasts. Eur. J. Biochem., 33, 253-257 (1973).
10. 2-fumigated leaves of spinach. Plant Cell Physiol., 21, 1193-1204 (1980).
11. Hasegawa, T., In MBI Report’93 (in Japanese), ed. Miyachi, S., Marine Biotechnology Institute, Tokyo, pp. 87-90 (1994).
12. Tanaka, K., Tolerance to herbicides and air pollutants. In “Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants”, eds. Foyer, C. H., and Mullineaux, P. M., CRC press, Boca Raton, pp. 365-379 (1994).
13. Sano, S., Ueda, M., Kitajima, S., Takeda, T., Shigeoka, S., Kurano, N., Miyachi, S., Miyake, C., and Yokota, A., Characterization of ascorbate peroxidases from unicellular red alga Galdieria partita. Plant Cell Physiol., 42, 433-440 (2001).
14. Mandelman, D., Jamal, J., and Poulos, T., Identification of two electron-transfer sites in ascorbate peroxidase using chemical modification, enzyme kinetics, and crystallography. Biochemistry, 37, 17610-17617 (1998).
15. Fuhrhop, J. H., and Smith, K. M., In “Porphyrins and Metalloporphyrins”, ed. Smith, K. M., Elsevier Scientific publishing Co., Amsterdam, p. 804 (1975).
16. Mittler, R., and Zilinskas, B. A., Purification and characterization of pea cytosolic ascorbate peroxidase. Plant Physiol., 97, 962-968 (1991).
17. Ishikawa, T., Yoshimura, K., Sakai, K., Tamoi, M., Takeda, T., and Shigeoka, S., Molecular characterization and physiological role of glyoxysome-bound ascorbate peroxidase from spinach. Plant Cell Physiol., 39, 23-34 (1998).
18. Shigeoka, S., Nakano, Y., and Kitaoka, S., Metabolism of hydrogen peroxide in Euglena gracilis Z by L-ascorbic acid peroxidase. Biochem J., 186, 377-380 (1980).
19. Shigeoka, S., Ohishi, T., Nakano, Y., and Kitaoka, S., Characterization and physiological function of glutathione reductase in Euglena gracilis Z. Biochem. J., 242, 511-515 (1987).
20. Ishikawa, T., Takeda, T., Shigeoka, S., Hirayama, O., and Mitsunaga, T., Hydrogen peroxide generation in organelles of Euglena gracilis. Phytochemistry, 33, 1297-1299 (1993).
21. Sivaraja, M., Goodin, D. B., Smith, M., and Hoffman, B. M., Identification by ENDOR of Trp191 as the free-radical site in cytochrome c peroxidase compound ES. Science, 245, 738-740 (1989).
22. Cheek, J., Mandelman, D., Poulos, T. L., and Dawson, J. H., A study of the K+-site mutant of as-corbate peroxidase: mutations of protein residues on the proximal side of the heme cause changes in iron ligation on the distal side. J. Biol. Inorg. Chem., 4, 64-72 (1999).
23. Hiner, A. N., Martinez, J. I., Arnao, M. B., Acosta, M., Turner, D. D., Lloyd, R. E., and Rodriguez-Lopez, J. N., Detection of a tryptophan radical in the reaction of ascorbate peroxidase with hydrogen peroxide. Eur. J. Biochem., 268, 3091-3098 (2001).
24. 2 fixation. Biochem. Biophys. Res. Commun., 233, 568-571 (1997).
25. Ausubel, F. M., Brent, R., Kingston, R. E., Moore, D. D., Seidman, J. G., Smith, J. A., and Struhl, K., Current Protocols in Molecular Biology. Greene Publishing Associates /John Wiley and Sons, New York (1997).
26. Sambrook, J., Fritsch, E. F., and Maniatis, T., Molecular Cloning: a Laboratory Manual 2nd Ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor (1989).
27. Hofmann, K., Bucher, P., Falquet, L., and Bairoch, A., The PROSITE database: its status in 1999. Nucleic Acids Res., 27, 215-219 (1999).
28. Thompson, J. D., Gibson, T. J., Plewniak, F., Jean-Mougin, F., and Higgins, D. G., The CLUSTAL X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res., 25, 4876-4882 (1997).
29. Pearson, W., and Lipman, D., Improved tools for biological sequence comparison. Proc. Natl. Acad. Sci. USA, 85, 2444-2448 (1988).
30. Yoshimura, K., Ishikawa, T., Nakamura, Y., Tamoi, M., Takeda, T., Tada, T., Nishimura, K., and Shigeoka, S., Comparative study on recombinant chloroplastic and cytosolic ascorbate peroxidase isozymes of spinach. Arch. Biochem. Biophys., 353, 55-63 (1998).
31. 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, 248-254 (1976).
32. Tomita, T., Tsuyama, S., Imai, Y., and Kitagawa, T., Purification of bovine soluble guanylate cyclase and ADP-ribosylation on its small subunit by bacterial toxins. J. Biochem., 199, 531-536 (1997).
33. Nakano, Y., and Asada, K., Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplasts. Plant Cell Physiol., 22, 867-880 (1981).
34. Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
35. Takeda, T., Yoshimura, K., Yoshii, M., Kanahoshi, H., Miyasaka, H., and Shigeoka, S., Molecular characterization and physiological role of ascorbate peroxidase from halotolerant Chlamydomonas sp. W80 strain. Arch. Biochem. Biophys., 376, 82-90 (2000).