Comparative studies on the activities of chitinase, beta-1,3-glucanase, peroxidase and phenylalanine ammonia lyase in the leaves of triticale and wheat infected with Stagonospora nodorum

• Autorzy: Rybka K , Arseniuk E. , Wisniewska J. , Raczynska-Bojanowska K.
• Języki publikacji: EN

Abstrakty

EN

The activities of chitinase, β-1,3-glucanase, peroxidase and phenylalanine ammonia lyase, constitutive and induced by Stagonospora nodorum were examined in the 10 – 14 day old seedlings of three triticale and two wheat cultivars under controlled environmental conditions and in flag leaves of two triticale cultivars in the field. Two S. nodorum isolates of different virulence were used. Both the constitutive and induced activities in triticale and wheat depended on genotype and in triticale the effect of growth conditions was also evidenced. The constitutive activities of chitinase, β-1,3-glucanase and peroxidase were several fold lower in flag triticale leaves in plants from the field than in the seedlings, growing under controlled conditions, but induction in the infected flag leaves was significantly more pronounced. In triticale genotypic differences in the response to infection were revealed only upon inoculation by S. nodorum isolate of higher virulence. The enzymatic activities increased several fold during successive days after the infection except for phenylalanine ammonia lyase. Induction of this enzyme was only transient and the activity decreased 48 or 96 h after infection when the activities of other enzymes were rising. In flag leaves in the field this activity was differentiated only after infection with more a virulent strain. A tendency appeared in triticale seedlings for association of the resistance to the pathogen with lower enzymatic constitutive activities. This relationship became more evident in triticale infected by S. nodorum and may imply that although the investigated enzymes are certainly involved in general, non-specific defense mechanism, they do not decide on the resistance to pathogen at least in the early stages of infection and cooperate with other factors in the complex pathogen-plant interaction. One can also assume that the enzymatic activities are associated with severity of infection rather than resistance to pathogen.

Słowa kluczowe

EN

phenylalanine; wheat; triticale; peroxidase; leaf; ammonia lyase; chitinase; Stagonospora nodorum; beta-1,3-glucanase

• Wydawca: -
• Czasopismo: Acta Physiologiae Plantarum
• Rocznik: 1998
• Tom: 20
• Numer: 1
• Opis fizyczny: p.59-66,fig.

Twórcy

autor

Rybka K

• Plant Breeding and Acclimatization Institute, Radzikow, PBX 1019, 00-950 Warsaw, Poland

autor

Arseniuk E.

autor

Wisniewska J.

autor

Raczynska-Bojanowska K.

Bibliografia

• Ahl Goy P., Felix G., Matraux J.P. and Meens F. 1992. Resistance to disease in the hybrid Nicotiana glutinosa × Nicotiana clebney is associated with high constitutive levels of β-1,3-glucanase, chitinase, peroxidase and polyphenoloxidase. Physiol. Mol. Plant Pathol. 41: 11–21.
• Alcazar M.D., Egea C., Espin A. and Candela M.E. 1995. Peroxidase isoenzymes in the defense response of Capsicum annuum to Phytophthora capsici. Physiol. Plant. 94: 736–742.
• Arseniuk E., Czembor H.J., Scharen A.L., Sowa W., Krysiak H. and Zimny J. 1994a. Response of triticale, wheat and rye germplasm lines to artificial inoculation with Stagonospora (Septoria) nodorum under controlled environmental and field conditions. Triticale Topics Newsletter (International Edition) 12: 13–23.
• Arseniuk E., Scharen A.L., Czembor H.J., Sowa W. and Krysiak H. 1991. Reaction of triticales from different geographic regions to Septoria nodorum blotch under climatic conditions of central Poland. Proc. 2nd Int. Triticale Symposium, Mexico, D. F.: CIMMIT: 252–255.
• Arseniuk E., Scharen A.L., Fried P.M. and Czembor H.J. 1994 b. Pathogenic interactions in X Triticosecale-Septoria ssp. systems. Hod. Rosl. Aklim. Nasien. 38: 101–108.
• Broglie K., Chet J., Holliday M., Cressman R., Biddle P., Knowlton S., Mauvais C.J. and Broglie R. 1991. Transgenic plants with enhanced resistance to fungal pathogen Rhizoctonie solani. Science, 254: 1194–1197.
• Bradford M.M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248–254.
• Collinge D.B., Kragh K.M., Mikkelsen J.D., Nielsen K.K., Rasmussen U. and Vad K. 1993. Plant chitinases. Plant J. 3(1): 31–40.
• Eyal Z., Scharen A.L., Prescott J.M. and van Ginkiel M. 1987. The Septoria diseases of wheat: concepts and methods of disease management. Mexico, D. F. CIMMYT.
• Hahlbrock K. and Scheel D. 1989. Physiology and molecular biology of phenylpropanoid metabolism. Ann. Rev. Plant Physiol. Plant Mol. Biol. 40: 347–369.
• Joos H.J. and Hahlbrook K. 1992. Phenylalanine ammonia-lyase in potato (Solanum tuberosum α). Eur. J. Biochem. 204: 621–629.
• Kim Y.J. and Hawang B.K. 1994. Differential accumulation of β-1,3-glucanase and chitinase isoforms in pepper stems infected by compatible and incompatible isolates of Phytophthora capsici. Physiol. Mol. Plant Pathol. 45(3): 195–209.
• Langrimini L.M., Vaughn J., Erb W.A. and Miller S.A. 1993. Peroxidase overproduction in tomato: wound-induced polyphenol deposition and disease resistance. Hort Science, 28(3): 218–221.
• Legrand M., Fritig B. and Hirth L. 1976. Enzymes of the phenylpropanoid pathway and the necrotic reaction of hypersensitive tobacco mosaic virus. Phytochem. 15: 1353–1359.
• Lehtinen M. 1993. Plant cell degrading enzymes of Septoria nodorum. Physiol. Mol. Plant Pathol. 3: 121–134.
• Liang X., Dron M., Cramer C.L., Dixon R.A. and Lamb Ch.J. 1989. Differential regulation of phenylalanine ammonia-lyase genes during plant development and by environmental cues. J. Biol. Chem. 264(24): 14486–14492.
• Liao Y.C., Kreuzaler F., Reisener H.J. and Tiburzy R. 1995. Characterization of a wheat class I b chitinase gene differentially induced in isogenic lines by infection with Puccinia graminis. Plant Sci. 103(2): 177–187.
• Leung D.R. 1992. Involvement of plant chitinase in sexual reproduction of higher plants. Phytochem. 31: 1899–19011.
• Mauch F., Hadwiger L.H. and Boller T. 1984. Ethylene: symptom not signal for the induction of chitinase and β-glucanase in pea pods by pathogens and elicitors. Plant Physiol. 76: 607–611.
• Mauch F., Hadwiger L.A. and Boller T. 1988. Antifungal Hydrolases in Pea Tissue. Plant Physiol. 87: 325–333.
• Mozzetti C., Ferraris L., Tamietti G. and Matta A. 1995. Variation in enzyme activities in leaves and cell suspensions as markers of incompatibility in different Phytophtora-pepper interactions. Physiol. Mol. Plant Path. 46: 95–109.
• Neuhaus J.M., Ahl Goy P., Hinz U., Flores U. and Meins F. 1991. High level expression of a tobacco chitinase gene in Nicotiana sylvestris. Susceptibility of a tobacco plants to Cercospora nicotianae. Plant Mol. Biol. 16: 141–151.
• Orr J.D., Edwards R. and Dixon R.A. 1993. Stress responses in alfalfa (Medicago sativa L.). Changes in the levels of phenylopropanoid pathway intermediates in relation to regulation of l-phenylalanine ammonia-lyase in elicitor-treated cell-suspension cultures. Plant Physiol. 101: 847–856.
• Patykowski J., Urbanek H. and Kaczorowska T. 1988. Peroxidase activity in leaves and wheat cultivars differing in resistance to Erysiphe graminis. J Phytopatol 122: 126–134.
• Pane S.Q., Ye X.S., and Kuc J. 1991. Association of β-1,3- glucanase activity and isoform pattern with systemic resistance to blue mold in tobacco induced by stem injection with Peronospora tabacina or leaf inoculation with tobacco mosaic virus. Physiol. Mol. Plant Pathol. 39: 25–39.
• Roulin S. and Buchara A.J. 1995. The induction of β-1,3-glucanase and other enzymes in ground leaves infected with Cercospora arachidicola. Physiol. Mol. Plant Pathol. 46: 471–489.
• Rybka K. and Arseniuk E. 1994. The enzyme response of triticale seedlings on infection by Stagonospora nodorum. Hod. Ros. Aklim. Nas. 38: 143–147.
• Rybka Z. 1989. Changes in cyanide-sensitive and cyanide-resistant oxygen uptake in crowns of winter wheat seedlings during hardening to frost. J. Plant Physiol. 134: 17–19.
• Schroder M., Hahlbrock K., Kombrink E. 1992. Temporal and spatial patterns of β-1,3-glucanase and chitinase induction in potato leaves infected by Phytophthora infestans Plant J. 2(2): 161–172.
• Scott-Craig J.S., Kerby K.B., Stein B.D. and Somerville S.C. 1995. Expression of an extracellular peroxidase that is induced in barley (Hordeum vulgare) by the powdery mildew pathogen (Erysiphe graminis f. sp. hordei). Physiol. Mol. Plant Pathol. 47(6): 407–418.
• Siefert F., Langebartels Ch., Boller T. and Grossmann K. 1994. Are ethylene and 1-amino-cyclo-propane-1-carboxylic acid involved in the induction of chitinase and β-1,3-glucanase activity in sunflower cellsuspension cultures. Planta, 192: 431–440.
• Van den Bulcke M., Bauw G., Castresana C., Van Montagu M. and Vandekerckhove J. 1989. Characterization of vacuolar and extracellular β-1,3-glucanases of tobacco: Evidence for a strictly compartmentalized plant defense system. Proc. Natl. Acad. Sci. USA, 86: 2673–2677.
• Wemmer T., Kaufman H., Kirch H.H., Schneider K., Lattspeich F. and Tompson R.D. 1994. The host abandoned soluble basic protein of the stylar transmitting track in potato is an endochitinase. Planta, 194: 264–273.