Biologia Plantarum

, Volume 42, Issue 2, pp 279–287 | Cite as

Benzothiadiazole as an Inducer of β-1,3-Glucanase and Chitinase Isozymes in Sugar Beet

  • L. Burketová
  • M. Šindelářová
  • L. Šindelář
Article

Abstract

The effect of benzothiadiazole (BTH) on protein synthesis was studied in sugar beet plants. Extracellular proteins induced by 0.025 % BTH were examined and their pattern was compared with that induced by sodium salicylate, chitosan, paraquat, AgNO3, and by tobacco necrosis virus. BTH induced synthesis of at least 9 acidic and 6 basic proteins; three of them appeared as acidic chitinase isozymes, three as acidic β-1,3-glucanase isozymes, three as basic chitinase isozymes, and one as a basic β-1,3-glucanase isozyme. One of the basic chitinase isozymes was found also in control plants. The most of the newly formed proteins was also induced by the other inducers under study regardless of the necrotic or symptomless reaction of plants. The benzothiadiazole proved to be an efficient inducer of proteins in sugar beet.

Bion chitosan paraquat pathogenesis-related proteins salicylic acid tobacco necrosis virus 

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References

  1. Berglund, L., Brunstedt, J., Nielsen, K.K., Chen, Z., Mikkelsen, J.D., Marcker, K.A.: A proline-rich chitinase from Beta vulgaris.-Plant mol. Biol. 27: 211–216, 1995.PubMedCrossRefGoogle Scholar
  2. Bernasconi, P., Locher, R., Pilet, P.E., Jolles, J., Jolles, P.: Purification and N-terminal amino-acid sequence of a basic lysozyme from Parthenocissus quinquefolia cultured in vitro.-Biochim. biophys. Acta 915: 254–260, 1987.Google Scholar
  3. Bradford, M.M.: A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein binding.-Anal. Biochem. 72: 248–254, 1976.PubMedCrossRefGoogle Scholar
  4. Broekaert, W.F., Parijs, J.V., Allen, A.K., Peumans, W.J.: Comparison of some molecular, enzymatic and antifungal properties of chitinases from thorn-apple, tobacco and wheat.-Physiol. mol. Plant Pathol. 33: 319–331, 1988.CrossRefGoogle Scholar
  5. Edreva, A.M.: Induction of "pathogenesis-related" proteins in tobacco leaves by physiological (non-pathogenic) disorders.-J. exp. Bot. 41: 701–703, 1990.Google Scholar
  6. El Ghaouth, A., Arul, J., Grenier, J., Asselin, A.: Antifungal activity of chitosan on two postharvest pathogens of strawbery fruits.-Phytopathology 82: 398–402, 1992.Google Scholar
  7. Ernst, D., Schraudner, M., Langebartels, C., Sandermann, H., Jr.: Ozone-induced changes of mRNA levels of β-1,3-glucanase, chitinase and "pathogenesis-related" protein 1b in tobacco plants.-Plant mol. Biol. 20: 673–682, 1992.PubMedCrossRefGoogle Scholar
  8. Fleming, T.M., McCarthy, D.A., White, R.F., Antoniw, J.F., Mikkelsen, J.D.: Induction and characterization of some of the pathogenesis-related proteins in sugar beet.-Physiol. mol. Plant Pathol. 39: 147–160, 1991.CrossRefGoogle Scholar
  9. Friedrich, L., Lawton, K.A., Ruess, W., Masner, P., Specker, N., Rella, H.G., Meier, B., Dincher, S., Staub, T., Uknes, S., Metraux, J.P., Kessmann, H.: A benzothiadiazole derivate induces SAR in tobacco.-Plant J. 10: 61–70, 1996.CrossRefGoogle Scholar
  10. Görlach, J., Volrath, S., Knauf-Beiter, G., Hengy, G., Beckhove, U., Kogel, K.H., Oostendorp, M., Staub, T., Ward, E., Kessmann, H., Ryals, J.: Benzothiadiazole, a novel class of inducers of systemic acquired resistance, activates gene expression and disease resistance in wheat.-Plant Cell 8: 629–643, 1996.PubMedCrossRefGoogle Scholar
  11. Gottschalk, T.E., Mikkelsen, J.D., Nielsen, J.E., Nielsen, K.K., Brunstedt, J.: Immunolocalization and characterization of a β-1,3-glucanase from sugar beet, deduction of its primary structure and nucleotide sequence by cDNA and genomic cloning.-Plant Sci. 132: 153–167, 1998.CrossRefGoogle Scholar
  12. Hadwiger, L.A., Wagoner, W.: Electrophoretic patterns of pea and Fusarium solani proteins synthesized in vitro or in vivo which characterize the compatible and incompatible interactions.-Physiol. Plant Pathol. 23: 153–162, 1983.CrossRefGoogle Scholar
  13. Hames, B.D., Rickwood, D. (ed.): Gel Electrophoresis of Proteins. A Practical Approach.-IRL Press, Oxford-New York-Tokyo 1990.Google Scholar
  14. Jacobsen, S., Mikkelsen, J.D., Hejgaard, J.: Characterization of two antifungal endochitinases from barley grain.-Physiol. Plant. 79: 554–562, 1990.CrossRefGoogle Scholar
  15. Kunz, W., Schurter, R., Maetzke, T.: The chemistry of benzothiadiazole plant activators.-Pestic. Sci. 50: 275–282, 1997.CrossRefGoogle Scholar
  16. Lawton, K.A., Friedrich, L., Hunt, M., Weymann, K., Delaney, T., Kessmann, H., Staub, T., Ryals, J.: Benzothiadiazole induces disease resistance in Arabidopsis by activation of the systemic acquired resistance signal transduction pathway.-Plant J. 10: 71–82, 1996.PubMedCrossRefGoogle Scholar
  17. Linthorst, H.J.M.: Pathogenesis-related proteins of plants.-Crit. Rev. Plant Sci. 10: 123–150, 1991.Google Scholar
  18. Malamy, J., Klessig, D.F.: Salicylic acid and plant disease resistance.-Plant J. 2: 643–654, 1992.Google Scholar
  19. Mauch, F., Hadwiger, L.A., Boller, T.: Ethylene: symptom, not signal for the induction of chitinase and β-1,3-glucanase in pea pods by pathogens and elicitors.-Plant Physiol. 66: 607–611, 1984.CrossRefGoogle Scholar
  20. Métraux, J.-P., Ahl Goy, P., Staus, T., Speich, J., Steinemann, A., Ryals, J., Ward, E.: Induced resistance in cucumber in response to 2,6-dichloroisonicotinic acid pathogens.-In: Hennecke, H., Verma, D.P.S., (ed.): Advances in Molecular Genetics of Plant-Microbe Interactions. Vol. 1. Pp. 432–439. Kluwer Academic Publishers, Dordrecht 1991.Google Scholar
  21. Nielsen, K.K., Bojsen, K., Collinge, D.B., Mikkelsen, J.D.: Induced resistance in sugar beet against Cercospora beticola: induction by dichloroisonicotinic acid is independent of chitinase and β-1,3-glucanase transcript accumulation.-Physiol. mol. Plant Pathol. 45: 89–99, 1994.CrossRefGoogle Scholar
  22. Nielsen, K.K., Mikkelsen, J.D., Kragh, K.M., Bojsen, K.: An acidic class III chitinase in sugar beet: Induction by Cercospora beticola, characterization, and expression in transgenic tobacco plants.-Mol. Plant Microbe Interact. 6: 495–506, 1993.PubMedGoogle Scholar
  23. Pierpoint, W.S., Tatham, A.S., Pappin, D.J.C.: Identification of virus induced protein of tobacco leaves that resemble the sweet-tasting protein thaumatin.-Physiol. mol. Plant Pathol. 31: 291–298, 1987.CrossRefGoogle Scholar
  24. Repka, V., Fisherová, I., Vanek, G.: Immunohistochemical localization of stress-related anionic peroxidase in germinating cucumber seeds.-Biol. Plant. 39: 467–472, 1997.CrossRefGoogle Scholar
  25. Roulin, S., Buchala, A.J.: The induction of 1,3-β-glucanases and other enzymes in groundnut leaves infected with Cercospora arachidicola.-Physiol. mol. Plant Pathol. 46: 471–489, 1995.CrossRefGoogle Scholar
  26. Ryals, J.A., Neunschwander, U.H., Willits, M.G., Molina, A., Steiner, H.-Y., Hunt, M.D.: Systemic acquired resistance.-Plant Cell 8: 1809–1819, 1996.PubMedCrossRefGoogle Scholar
  27. Seetharaman, K., Waniska, R.D., Rooney, W.: Physiological changes in sorghum antifungal proteins.-J. Agr. Food Chem. 44: 2435–2441, 1996.CrossRefGoogle Scholar
  28. Shimoni, M.: A method for activity staining of peroxidase and β-1,3-glucanase isozymes in polyacrylamide electrophoresis gels.-Anal. Biochem. 220: 36–38, 1994.PubMedCrossRefGoogle Scholar
  29. Steiner, A.A.: The universal nutrient solution.-In: Proc. Sixth Int. Congress on Soilless Culture, Lunteren, International Society for Soilless Culture. Pp. 633–650. Pudoc, Wageningen 1984.Google Scholar
  30. Tamás, L., Huttová, J., Zigová, Z.: Accumulation of stress-proteins in intercellular spaces of barley leaves induced by biotic and abiotic factors.-Biol. Plant. 39: 387–394, 1997.CrossRefGoogle Scholar
  31. Trudel, J., Asselin, A.: Detection of chitinase activity after polyacrylamide gel electrophoresis.-Anal. Biochem. 178: 362–366, 1989.PubMedCrossRefGoogle Scholar
  32. Uknes, S., Mauch-Mani, B., Moyer, M., Potter, S., Williams, S., Dincher, S., Chandler, D., Slusarenko, A., Ward, E., Ryals, J.: Acquired resistance in Arabidopsis.-Plant Cell 4: 645–656, 1992.PubMedCrossRefGoogle Scholar
  33. Van Loon, L.C., Antoniw, J.F.: Comparison of the effects of salicylic acid and ethephon with virus-induced hypersensitivity and acquired resistance.-Neth. J. Plant Pathol. 88: 237–256, 1982.CrossRefGoogle Scholar
  34. Van Loon, L.C.: Pathogenesis-related proteins.-Plant. mol. Biol. 4: 11–116, 1985.Google Scholar
  35. Ward, E.R., Uknes, S.J., Williams, S.C., Dincher, S.S., Wiederhold, D.L., Alexander, D.C., Ahl-Goz, P., Metraux, J.-P., Ryals, J.A.: Coordinate gene activity in response to agents that induce systemic acquired resistance.-Plant Cell 3: 1085–1094, 1991.PubMedCrossRefGoogle Scholar

Copyright information

© Kluwer Academic Publishers 1999

Authors and Affiliations

  • L. Burketová
    • 1
  • M. Šindelářová
    • 1
  • L. Šindelář
    • 1
  1. 1.Institute of Experimental BotanyAcademy of Sciences of the Czech Republic, Na Karlovce laPraha 6Czech Republic

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