Skip to main content
SpringerLink
Log in

Physiological and Biochemical Characteristics of Tobacco Transgenic Plants Expressing Bacterial Dioxygenase

  • Published:
Russian Journal of Plant Physiology Aims and scope Submit manuscript

Abstract

Expression of the 1,2-dihydroxynaphthalene dioxygenase (nahC) gene from Pseudomonas putida in tobacco transgenic plants produces notable phenotypic and biochemical changes: retarded growth and rooting and earlier flowering; chlorotic and necrotic spots on leaves; and a threefold increase in the total phenolics in the leaves of 6-week-old plants (94.51 μg/g fr wt as compared to 33.18 μg/g fr wt in the control) and in the phenylalanine-ammonia lyase activity in 4-week-old plants (0.035 U/g fr wt as compared to 0.014 U/g in the control plants of the same age). The transgenic plants expressing the nahC bacterial gene may serve as a model to study the putative functions of dioxygenases and phenol compounds in plant growth, development, and stress responses.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

REFERENCES

  1. Wightman, F., Metabolism and Biosynthesis of Indole-3-Acetic Acid and Related Indole Compounds in Plants, Can. J. Bot., 1962, vol. 40, pp. 689-718.

    Google Scholar 

  2. Mayer, A.M. and Harel, E., Polyphenol Oxidases in Plants, Phytochemistry, 1979, vol. 18, pp. 193-215.

    Google Scholar 

  3. Chapple, C. and Carpita, N., Plant Cell Walls as Targets for Biotechnology, Curr. Opin. Biol., 1998, vol. 1, pp. 179-185.

    Google Scholar 

  4. Kosuge, T., The Role of Phenolics in Host Response to Infection, Annu. Rev. Phytopathol., 1969, vol. 7, pp. 195-222.

    Google Scholar 

  5. Harborne, J.B., Plant Phenolics, Encycl. Plant Physiol., New Ser., vol. 8, Bell, E.A. and Charewood, B.V., Eds., Berlin: Springer-Verlag, 1980, pp. 329-402.

    Google Scholar 

  6. Tsoi, T.V., Kosheleva, I.A., Zamaraev, V.S., Trelina, O.L., Selifonov, S.A., Zakharova, M.U., Starovoitov, I.I., and Boronin, A.M., Cloning and Expression of Pseudomonas putida Gene Controlling Catechol-2,3-Oxygenase Activity in Escherichia coli Cells, Genetika, 1988, vol. 24, pp. 1550-1561.

    Google Scholar 

  7. Mordukhova, E.A., Sokolov, S.L., Kochetkov, V.V., Kosheleva, I.A., Zelenkova, N.F., and Boronin, A.M., Involvement of Naphthalene Dioxygenase in Indole-3-Acetic Acid Biosynthesis by Pseudomonas putida, FEMS Microbiol. Lett., 2000, vol. 190, pp. 279-285.

    Google Scholar 

  8. Maleck, K. and Lawton, K., Plant Strategies for Resistance to Pathogens, Curr. Opin. Biotechnol., 1998, vol. 9, pp. 208-213.

    Google Scholar 

  9. Van Lijsebettens, M. and Valvekens, D., Tobacco Leaf Disk Infection with Agrobacterium tumefaciens, EMBO Practical Course on Plant Molecular Biology, Gent (Belgium), 1987, pp. 15-18.

  10. Lazo, G.R., Stein, P.A., and Ludwig, R.A., DNA Transformation-Competent Arabidopsis Genomic Library in Agrobacterium, Biotechnology, 1991, vol. 9, pp. 963-967.

    Google Scholar 

  11. Deblaere, R., Reynaerts, A., Hofte, H., Hernalsteens, J.P., Leemans, J., and van Montagu, M., Vector for Cloning in Plant Cells, Methods Enzymol., 1987, vol. 153, pp. 277-292.

    Google Scholar 

  12. Sambrook, J., Fritsch, E.F., Maniatis, T., Molecular Cloning: A Laboratory Manual, Cold Spring Harbor: Cold Spring Harbor Lab., 1989.

    Google Scholar 

  13. Logmann, J., Schell, J., and Willmitzer, L., Improved Method for the Isolation of RNA from Plant Tissue, Anal. Biochem., 1987, vol. 163, pp. 16-20.

    Google Scholar 

  14. Church, G. and Gilbert, W., Genomic Sequencing, Proc. Natl. Acad. Sci. USA, 1984, vol. 81, pp. 1991-1995.

    Google Scholar 

  15. Cvikrová, M., Hrubcová, M., Meravy, L., and Pospišil, F., Changes in the Content of Phenolic Substances during the Growth of Nicotiana tabacum Cell Suspension Culture, Biol. Plant., 1988, vol. 30, pp. 185-192.

    Google Scholar 

  16. 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., 1976, vol. 72, pp. 248-254.

    Google Scholar 

  17. Flurkey, W., Polyphenoloxidase in Higher Plants, Plant Physiol., 1986, vol. 81, pp. 614-618.

    Google Scholar 

  18. Hyodo, H. and Yang, S.F., Ethylene-Enhanced Synthesis of Phenylalanine-Ammonia Lyase in Pea Seedlings, Plant Physiol., 1971, vol. 47, pp. 765-770.

    Google Scholar 

  19. Shlyk, A.A., Determination of Chlorophylls and Carotenoids in the Extracts from Green Leaves, Biokhimicheskie metody v fiziologii rastenii (Biochemical Methods in Plant Physiology), Pavlinova, O.A., Ed., Moscow: Nauka, 1971, pp. 154-171.

    Google Scholar 

  20. Glawischnig, E., Tomas, A., Eisenreich, W., Spiteller, P., Bacher, A., and Gierl, A., Auxin Biosynthesis in Maize Kernels, Plant Physiol., 2000, vol. 123, pp. 1109-1119.

    Google Scholar 

  21. Binns, A.N., Chen, R.H., Wood, H.N., and Lynn, D.G., Cell Division Promoting Activity of Naturally Occurring Dehydrodiconiferyl Glucosides: Do Cell Wall Components Control Cell Division?, Proc. Natl. Acad. Sci. USA, 1987, vol. 84, pp. 980-984.

    Google Scholar 

  22. Elkind, Y., Liang, X., Dron, M., and Lamb, C., Annual Report of Plant Biology Laboratory. Salk Institute for Biological Studies, California (USA), 1988.

  23. Tamagnone, L., Merida, A., Parr, A., Mackay, S., Culianez-Macia, F.A., Roberts, K., and Martin, C., The AmMYB308 and AmMYB330 Transcription Factors from Antirrhinum Regulate Phenylpropanoid and Lignin Biosynthesis in Transgenic Tobacco, Plant Cell, 1998, vol. 10, pp. 135-154.

    Google Scholar 

  24. Tamagnone, L., Merida, A., Stacey, N., Plaskitt, K., Parr, A., Chang, C.-F., Lynn, D., Dow, J.M., Roberts, K., and Martin, C., Inhibition of Phenolic Acid Metabolism Results in Precocious Cell Death and Altered Cell Morphology in Leaves of Transgenic Tobacco Plants, Plant Cell, 1998, vol. 10, pp. 1801-1816.

    Google Scholar 

  25. Molgaafd, P. and Rayn, H., Evolutionary Aspects of Caffeoyl Esters Distribution in Dicotyledons, Phytochemistry, 1988, vol. 27, pp. 2411-2421.

    Google Scholar 

  26. Hisaminato, H., Murata, M., and Homma, S., Relationship between the Enzymatic Browning and Phenylalanine-Ammonia Lyase Activity of Cut Lettuce, and the Prevention of Browning by Inhibitors of Polyphenol Biosynthesis, BioSci. Biotech. Biochem., 2001, vol. 65, pp. 1016-1021.

    Google Scholar 

  27. Guerra, D., Anderson, A.J., and Salisbury, F.B., Reduced Phenylalanine-Ammonia Lyase and Tyrosine-Ammonia Lyase Activities and Lignin Synthesis in Wheat Grown under Low Pressure Sodium Lamps, Plant Physiol., 1985, vol. 78, pp. 126-130.

    Google Scholar 

  28. Basak, M., Sharma, M., and Chakraborty, U., Biochemical Responses of Camellia sinensis (L.) O. Kuntze to Heavy Metal Stress, J. Environ. Biol., 2001, vol. 22, pp. 37-41.

    Google Scholar 

  29. Duke, S.O. and Vaught, K.C., Lack of Involvement of Polyphenol Oxidase in Ortho-Hydroxylation of Phenolic Compounds in Mung Been Seedling, Physiol. Plant., 1982, vol. 54, pp. 381-385.

    Google Scholar 

  30. Cantos, E., Espin, J.C., and Tomas-Barberan, F.A., Effect of Wounding on Phenolic Enzymes in Six Minimally Processed Lettuce Cultivars upon Storage, J. Agric. Food Chem., 2001, vol. 49, pp. 322-330.

    Google Scholar 

  31. Hernandez, A. and Cano, M.P., High-Pressure and Temperature Effects on Enzyme Inactivation in Tomato Puree, J. Agric. Food Chem., 1998, vol. 46, pp. 266-270.

    Google Scholar 

  32. Mayer, A.M., Polyphenol Oxidases in Plant-Recent Progress, Phytochemistry, 1987, vol. 26, pp. 11-20.

    Google Scholar 

  33. Mokronosov, A.T. and Gavrilenko, V.F., Fotosintez: Fiziologo-biokhimicheskie aspekty: Uchebnik (Photosynthesis: Physiological and Biochemical Aspects. Manual), Moscow: Mosk. Gos. Univ., 1992.

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Vavilov Institute of General Genetics, Russian Academy of Sciences, ul. Gubkina 3, Moscow, 119991, Russia

    E. S. Piruzian, I. V. Goldenkova, N. S. Kobets, V. L. Mett & K. A. Musiichuk

  2. Botanical Garden, National Academy of Sciences, Minsk, Belarus

    A. A. Lenets

  3. Institute of Experimental Botany, Czech Academy of Sciences, Praha, Czech Republic

    M. Cvikrová & I. Macháčková

Authors
  1. E. S. Piruzian
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. I. V. Goldenkova
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. A. A. Lenets
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. M. Cvikrová
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. I. Macháčková
    View author publications

    You can also search for this author in PubMed Google Scholar

  6. N. S. Kobets
    View author publications

    You can also search for this author in PubMed Google Scholar

  7. V. L. Mett
    View author publications

    You can also search for this author in PubMed Google Scholar

  8. K. A. Musiichuk
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Piruzian, E.S., Goldenkova, I.V., Lenets, A.A. et al. Physiological and Biochemical Characteristics of Tobacco Transgenic Plants Expressing Bacterial Dioxygenase. Russian Journal of Plant Physiology 49, 817–822 (2002). https://doi.org/10.1023/A:1020977931969

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1023/A:1020977931969

Search

Navigation