Identification of Zantedeschia aethiopica Cat1 and Cat2 catalase genes and their expression analysis during spathe senescence and regreening

Plant Science

Volumn 167, Issue 4, 2004, Pages 889-898

  Lino Neto, Teresa ^a   Piques, Maria Conceição ^a   Barbeta, Cátia ^a   Sousa, Manuel F ^a   Tavares, Rui M ^a   Pais, Maria Salomé ^b  

^a UNIVERSITY OF MINHO   (Portugal)

^b ICAT   (Portugal)

Author keywords

Catalase; Peroxisomal metabolism; Peroxisomal targeting signal; Regreening; Senescence; Zantedeschia aethiopica

Indexed keywords

GENES; GENETIC ENGINEERING; PLANTS (BOTANY);

GATALASE GENES; PLANT ENCODE CATALASE;

ENZYMES;

ARACEAE; EMBRYOPHYTA; FELIS CATUS; ORYZA SATIVA; ZANTEDESCHIA AETHIOPICA; ZEA; ZEA MAYS;

EID: 3543068245     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2004.05.030     Document Type: Article

References (57)

1. J.G. Scandalios, Regulation and properties of plant catalases, in: C.H. Foyer, P.M. Mullineaux (Eds.), Causes of Photooxidative Stress and Amelioration of Defense Systems in Plants, CRC Press, Boca Raton, 1994, pp. 275-315.
2. M. Heinze, B. Gerhardt, Plant catalases, in: A. Baker, I.A. Graham, (Eds.), Plant Peroxisomes, Kluwer Academic Publishers, Dordrecht, 2002, pp. 103-140.
3. Scandalios J.G. Response of plant antioxidant defense genes to environmental stress. Adv. Genet. 28:1990;1-41
4. 3 plants. EMBO J. 16:1997;4806-4816
5. 2. Plant Physiol. 89:1989;952-957
6. Polidoros A.N., Scandalios J.G. Response of the maize catalases to light. Free Radical Biol. Med. 23:1997;497-504
7. Scandalios J.G., Acevedo A., Ruzsa S. Catalase gene expression in response to chronic high temperature stress in maize. Plant Sci. 156:2000;103-110
8. Kunce C.M., Trelease R.N. Heterogeneity of catalase in maturing and germinated cotton seeds. Plant Physiol. 81:1986;1134-1139
9. Eising R., Gerhardt B. Catalase degradation in sunflower cotyledons during peroxisome transition from glyoxysomes to leaf peroxisomal function. Plant Physiol. 84:1987;225-232
10. Havir E.A., McHale N.A. Biochemical and developmental characterization of multiple forms of catalase in tobacco leaves. Plant Physiol. 84:1987;450-455
11. Huang D., Scandalios J.G., Skadsen R.W., Tsaftaris A.S. Non-coordinate genetic alterations in the expression of catalase and other glyoxysomal enzymes during maize development. J. Exp. Biol. 37:1986;1189-1200
12. Esaka M., Yamada N., Kitabayashi M., Setoguchi Y., Tsugeki R., Kondo M., Nishimura M. cDNA cloning and differential gene expression of three catalases in pumpkin. Plant Mol. Biol. 33:1997;141-155
13. Frugoli J.A., Zhong H.H., Nuccio M.L., McCourt P., McPeek M.A., Thomas T.L., McClung C.R. Catalase is encoded by a multigene family in Arabidopsis thaliana (L.) Heynh. Plant Physiol. 112:1996;327-336
14. Abler M.L., Scandalios J.G. Isolation and characterization of a genomic sequence encoding the maize Cat3 catalase gene. Plant Mol. Biol. 22:1993;1031-1038
15. Guan L., Polidoros A.N., Scandalios J.G. Isolation, characterization and expression of the maize Cat2 catalase gene. Plant Mol. Biol. 30:1996;913-924
16. Guan L., Scandalios J.G. Characterization of the catalase antioxidant defense gene Cat1 of maize, and its developmentally regulated expression in transgenic tobacco. Plant J. 3:1993;527-536
17. Willekens H., Villarroel R., Van Montagu M., Inzé D., Van Camp W. Molecular identification of catalases from Nicotiana plumbaginifolia (L.). FEBS Lett. 352:1994;79-83
18. Higo K., Higo H. Cloning and characterization of the rice CatA catalase gene, a homologue of the maize Cat3 gene. Plant Mol. Biol. 30:1996;505-521
19. Iwamoto M., Maekawa M., Saito H., Higo H., Higo K. Evolutionary relationship of plant catalase genes inferred from exon-intron structures: isozyme divergence after the separation of monocots and dicots. Theor. Appl. Genet. 97:1998;9-19
20. Redinbaugh M.G., Wadsworth G.J., Scandalios J.G. Characterization of catalase transcripts and their differential expression in maize. Biochim. Biophys. Acta. 951:1988;104-106
21. Suzuki M., Ario T., Hattori T., Nakamura K., Asahi T. Isolation and characterization of two tightly linked catalase genes from castor bean that are differentially regulated. Plant Mol. Biol. 25:1994;507-516
22. Willekens H., Langebartels C., Tiré C., Van Montagu M., Inzé D., Van Camp W. Differential expression of catalase genes in Nicotiana plumbaginifolia (L.). Proc. Natl. Acad. Sci. USA. 91:1994;10450-10454
23. Skadsen R.W., Schulze-Lefert P., Herbst J.M. Molecular cloning, characterization and expression analysis of two catalase isozyme genes in barley. Plant Mol. Biol. 1995:1995;1005-1014
24. McClung C.R. Regulation of catalases in Arabidopsis. Free Radical Biol. Med. 23:1997;489-496
25. Iwamoto M., Higo H., Higo K. Differential diurnal expression of rice catalase genes: the 5′-flanking region of CatA is not sufficient for circadian control. Plant Sci. 151:2000;39-46
26. Wadsworth G.J., Scandalios J.G. Differential expression of the maize catalase genes during kernel development: the role of steady-state mRNA levels. Dev. Genet. 10:1989;304-310
27. Scandalios J.G., Tong W.F., Roupakias D.G. Cat3, a 3rd gene locus coding for a tissue-specific catalase in maize (Zea mays): genetics, intracellular location and some biochemical properties. Mol. Gen. Genet. 179:1980;33-42
28. Pais M.S.S., Novais M.C., Abreu I. Sur le reverdissement de la spathe de Zantedeschia aethiopica au cours de la fruitification. Hormones du type kinine. II - Effets sur le taux en protéines: taxes photosynthétique et respiratoire. Port. Acta Biol. (Ser. A). 15:1976;1-22
29. Melo N., Tavares R.M., Morais F., Barroso J.G., Pais M.S.S. Lipid composition of thylakoid membranes from leaves and regreened spathes of Zantedeschia aethiopica. Phytochemistry. 40:1995;1367-1371
30. Tavares R.M., Karmali A., Clemente A., Pais M.S. Production and characterization of a specific rubisco monoclonal antibody, and its use in rubisco quantification during Zantedeschia aethiopica spathe development. Hybridoma. 18:1999;203-209
31. 3-trans-hexadecenoic acid in photochemical activity. Phytochemistry. 47:1998;979-984
32. Mollenhauer H.H. Plastic embedding for use in electron microscopy. Stain Technol. 39:1964;111-114
33. Silverberg B.A., Sawa T. An ultrastructural and cytochemical study of microbodies in the genus Nitella (Characeae). Can. J. Bot. 51:1973;2025-2032
34. Volokita M. The carboxy-terminal end of glycolate oxidase directs a foreign protein into tobacco leaf peroxisomes. Plant J. 1:1991;361-366
35. H. Aebi, Catalase, in: H.U. Bergmeyer (Ed.), Enzymes 1: Oxidoreductases, Transferases, Verlag Chemie, New York, 1983, pp. 273-286.
36. J.B.J. Robinson, L.G. Brent, B. Sumegi, P.A. Srere, An enzymatic approach to the study of Krebs tricarboxylic acid cycle, in: V.M. Darley-Usmar, D. Rickwood, M.T. Wilson (Eds.), Mitochondria - A Practical Approach, IRL Press, Oxford, 1987, pp. 153-170.
37. Liang Z., Yu C., Huang A.H.C. Conversion of glycerate to serine in intact spinach leaf peroxisomes. Arch. Biochem. Biophys. 233:1984;393-401
38. Zelitch I. Synthesis of glycolate from pyruvate via isocitrate lyase by tobacco leaves in light. Plant Physiol. 86:1988;463-468
39. Sedmak J.J., Grossberg S.E. A rapid, sensitive, and versatile assay for protein using Coomassie Brilliant Blue G250. Anal. Biochem. 79:1977;544-552
40. Arnon D.I. Copper enzymes in chloroplasts. Polyphenoloxidases in Beta vulgaris. Plant Physiol. 24:1949;1-14
41. J. Sambrook, E.F. Fritsch, T. Maniatis, Molecular Cloning: a Laboratory Manual, second ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, 1989.
42. Fita I., Rossmann M.G. The active center of catalase. J. Mol. Biol. 185:1985;21-37
43. Murthy M.R.N., Reid T.J.I., Sicignano A., Tanaka N., Rossmann M.G. Structure of beef liver catalase. J. Mol. Biol. 152:1981;465-499
44. Guan L., Scandalios J.G. Molecular evolution of maize catalases and their relationship to other eukaryotic and prokaryotic catalases. J. Mol. Evol. 42:1996;570-579
45. Klotz M.G., Klassen G.R., Loewen P.C. Phylogenetic relationships among prokaryotic and eukaryotic catalases. Mol. Biol. Evol. 14:1997;951-958
46. González E. The C-terminal domain of plant catalases: implications for a glyoxysomal targeting sequence. Eur. J. Biochem. 199:1991;211-215
47. Kamigaki A., Mano S., Terauchi K., Nishi Y., Tachibe-Kinoshita Y., Nito K., Kondo M., Hayashi M., Nishimura M., Esaka M. Identification of peroxisomal targeting signal of pumpkin catalase and the binding analysis with PTS1 receptor. Plant J. 33:2003;161-175
48. Mullen R.T., Lee M.S., Trelease R.N. Identification of the peroxisomal targeting signal for cottonseed catalase. Plant J. 12:1997;313-322
49. Frugoli J.A., McPeek M.A., Thomas T.L., McClung C.R. Intron loss and gain during evolution of the catalase gene family in Angiosperms. Genetics. 149:1998;355-365
50. D. Huang, R.N. Trelease, T.S.J. Moore, Plant Peroxisomes. Academic Press, New York, 1983.
51. Mullen R.T., Lee M.S., Flynn C.R., Trelease R.N. Diverse amino acid residues function within the type 1 peroxisomal targeting signal. Implication for the role of accessory residues upstream of the type 1 peroxisomal targeting signal. Plant Physiol. 115:1997;881-889
52. De Bellis L., Picciarelli L., Pistelli L., Alpi A. Localization of glyoxylate-cycle marker enzymes in peroxisomes of senescent leaves and green cotyledons. Planta. 180:1990;435-439
53. Gut H., Matile P. Apparent induction of key enzymes of the glyoxylic acid cycle in senescent barley leaves. Planta. 176:1988;548-550
54. Landolt R., Matile P. Glyoxysome-like microbodies in senescent spinach leaves. Plant Sci. 72:1990;159-163
55. Nishimura M., Takeuchi Y., De Bellis L., Hara-Nishimura I. Leaf peroxisomes are directly transformed to glyoxysomes during senescence of pumpkin cotyledons. Protoplasma. 175:1993;131-137
56. Willekens H., Inzé D., Van Montagu M., Van Camp W. Catalases in plants. Molecul. Breed. 1:1995;207-228
57. Guan L.M., Scandalios J.G. Catalase gene expression in response to auxin-mediated developmental signals. Physiol. Plant. 114:2002;288-295