Russian Journal of Plant Physiology

, Volume 53, Issue 4, pp 469–473

Specific features of oxidative stress in the chilled tobacco plants following transformation with the desC gene for acyl-lipid Δ9-desaturase from Synechococcus vulcanus

  • V. N. Popov
  • N. V. Kipaikina
  • N. V. Astakhova
  • T. I. Trunova


Tobacco plants (Nicotiana tabacum L.) transformed with the desC gene for acyl-lipid Δ9-desaturase from a thermophilic cyanobacterium Synechococcus vulcanus were cultivated on the agarized Murashige and Skoog medium at 22°C and a 16-h photoperiod. Tobacco plants transformed with an empty binary vector pGA482 served as the control. The investigations showed that, in contrast to the control, transgenic plants maintained a higher activity of antioxidant enzymes during 2-h incubation at 2°C; as a result, these plants resisted more efficiently the accumulation of reactive oxygen species and reduced the rate of the lipid peroxidation. The activity of antioxidant enzymes in the transformed plants is apparently related to the operation of the introduced desC gene for acyl-lipid Δ9-desaturase because the enhanced activity of the latter increased the relative content of polyunsaturated FAs in membrane lipids and in this way promoted the liquid state of membranes during the chilling period. These changes helped preserve the cellular homeostasis and thereby maintain the steady synthesis of antioxidant enzymes at hypothermic conditions; as a result, cold resistance of transformed tobacco plants increased.

Key words

Nicotiana tabacum transgenic plants acyl-lipid desaturase antioxidant enzymes cold resistance 



fatty acid




peroxidation of lipids


reactive oxygen species


superoxide dismutase.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Hariadi, P. and Parkin, K.L., Chilling Induced Oxidative Stress in Cucumber Seedling, J. Plant Physiol., 1993, vol. 141, pp. 733–738.Google Scholar
  2. 2.
    Prasad, T.K., Anderson, M.D., Martin, B.A., and Stewart, C.R., Evidence for Chilling-Induced Oxidative Stress in Maize Seedlings and a Regulatory Role for Hydrogen Peroxide, Plant Cell, 1994, vol. 6, pp. 65–74.PubMedCrossRefGoogle Scholar
  3. 3.
    Lukatkin, A.S., Kholodovoe povrezhdenie teplolyubivykh rastenii i okislitel’nyi stress (Cold Damage to Chilling-Sensitive Plants and Oxidative Stress), Saransk: Mordov. Gos. Univ., 2002.Google Scholar
  4. 4.
    Merzlyak, M.N., Aktivirovannyi kislorod i okislitel’nye protsessy v membranakh rastitel’noi kletki (Activated Oxygen and Oxidative Processes in Plant Cell Membranes), Itogi Nauki i Tekhniki, Ser. Fiziol. Rast., 1989, vol. 6.Google Scholar
  5. 5.
    Vladimirov, Yu.A. and Archakov, A.P., Perekisnoe okislenie lipidov biologicheskikh membran (Lipid Peroxidation in Biological Membranes), Moscow: Nauka, 1972.Google Scholar
  6. 6.
    Mazliak, P., Glyco-and Phospholipids of Biomembranes in Higher Plants, Lipids and Lipid Polymers in Higher Plants, Berlin: Springer-Verlag, 1977, pp. 48–77.Google Scholar
  7. 7.
    Baraboi, V.A., Mechanisms of Stress and Lipid Peroxidation, Usp. Sovrem. Biol., 1991, vol. 111, pp. 923–931.Google Scholar
  8. 8.
    Orlova, I.V., Serebriiskaya, T.S., Popov, V.N., Merkulova, N.V., Nosov, A.M., Trunova, T.I., Tsydendambaev, V.D., and Los, D.A., Transformation of Tobacco with a Gene for the Thermophilic Acyl-Lipid Desaturase Enhances the Chilling Tolerance of Plants, Plant Cell Physiol., 2003, vol. 44, pp. 447–450.PubMedCrossRefGoogle Scholar
  9. 9.
    Popov, V.N., Orlova, I.V., Kipaikina, N.V., Serebriiskaya, T.S., Merkulova, N.V., Nosov, A.M., Trunova, T.I., Tsydendambaev, V.D., and Los, D.A., The Effect of Tobacco Plant Transformation with a Gene for Acyl-Lipid Δ9-Desaturase from Synechococcus vulcanus on Plant Chilling Tolerance, Fiziol. Rast. (Moscow), 2005, vol. 52, pp. 747–750 (Russ. J. Plant Physiol., Engl. Transl., pp. 664–667).Google Scholar
  10. 10.
    Brennan, T. and Frenkel, C., Involvement of Hydrogen Peroxide in the Regulation of Senescence in Pear, Plant Physiol., 1977, vol. 59, pp. 411–416.PubMedCrossRefGoogle Scholar
  11. 11.
    Zhirov, V.K., Merzlyak, M.N., and Kuznetsov, L.V., Lipid Peroxidation in Membranes from Cold-Resistant Plants under Below-Zero Temperature Damage, Fiziol. Rast. (Moscow), 1982, vol. 29, pp. 1045–1052 (Sov. Plant Physiol., Engl. Transl.).Google Scholar
  12. 12.
    Beauchamp, Ch. and Fridovich, I., Superoxide Dismutase Improved Assays and an Assay Applicapable to Acrylamide Gels, Anal. Biochem., 1971, no. 3, pp. 276–287.Google Scholar
  13. 13.
    Kumar, C.N. and Knowles, N., Changes in Lipid Peroxidation and Lipolytic and Free-Radical Scavenging Enzyme during Aging and Sprouting of Potato (Solanum tuberosum L.) Seed-Tubers, Plant Physiol., 1993, vol. 102, pp. 115–124.PubMedGoogle Scholar
  14. 14.
    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.PubMedCrossRefGoogle Scholar
  15. 15.
    Dospekhov, B.A., Metodika opytnogo dela (Methods for Experiments), Moscow: Kolos, 1977.Google Scholar
  16. 16.
    Chen, Yi-Zhu and Patterson, B.D., The Effect of Chilling Temperature on the Level of Superoxide Dismutase, Catalase and Hydrogen Peroxide in Some Plant Leaves, Acta Phytophysiol. Sin., 1988, vol. 14, pp. 323–328.Google Scholar
  17. 17.
    Gianinetti, A., Cantoni, M., Lorenzoni, C., Salamini, F., and Marocco, A., Altered Levels of Antioxidant Enzymes Associated with Two Mutations in Tomato, Physiol. Plant., 1993, vol. 89, pp. 157–164.CrossRefGoogle Scholar
  18. 18.
    Okane, D., Gill, V., Boyd, P., and Burdon, B., Chilling, Oxidative Stress and Antioxidant Responses in Arabidopsis thaliana Callus, Planta, 1996, vol. 198, pp. 371–377.CrossRefGoogle Scholar
  19. 19.
    Zhang, J.X., Cui, S.P., Li, J.M., Wei, J.K., and Kirkham, M.B., Protoplasmic Factors, Antioxidant Responses, and Chilling Resistance in Maize, Plant Physiol. Biochem., 1995, vol. 33, pp. 567–575.Google Scholar

Copyright information

© MAIK “Nauka/Interperiodica” 2006

Authors and Affiliations

  • V. N. Popov
    • 1
  • N. V. Kipaikina
    • 1
  • N. V. Astakhova
    • 1
  • T. I. Trunova
    • 1
  1. 1.Timiryazev Institute of Plant PhysiologyRussian Academy of SciencesMoscowRussia

Personalised recommendations