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Differential response of Cu,Zn superoxide dismutases in two pea cultivars during a short-term exposure to sulfur dioxide

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Abstract

Pea cultivars Progress and Nugget have been shown previously to be differentially sensitive with respect to apparent photosynthesis in a short-term exposure to 0.8 μl/l SO2. One possible contributing factor to the relative insensitivity of apparent photosynthesis of Progress to SO2 is an increase in superoxide dismutase (SOD) activities. We show here that both chloroplastic and cytoplastic Cu,Zn-SOD proteins increased in Progress on exposure to sulfur dioxide whereas both proteins decreased in Nugget. The increase in cytosolic Cu,Zn-SOD protein was greater than that of chloroplastic Cu,Zn-SOD protein. Using a gene-specific probe for the plastid SOD, northern blot analysis revealed an initial decrease in transcript abundance of the chloroplastic Cu,Zn-SOD gene in Progress on exposure to SO2 with an eventual recovery to pre-exposure levels. The transcript levels of the chloroplastic Cu,Zn-SOD decreased in Nugget over the time period of the exposure. These results suggest that a combination of translational and post-translational mechanisms may be involved in SO2-induced changes in cytosolic and plastidic Cu,Zn-SODs in pea.

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References

  1. Alscher RG, Madamanchi NR, Cramer CL: Protective mechanisms in the chloroplast stroma. In: Pell E, Steffen K (eds) Active Oxygen/Oxidative Stress and Plant Metabolism, pp. 145–155. American Society of Plant Physiologists, Rockville, TN (1991).

    Google Scholar 

  2. Alscher RG, Bower J, Zipfel W: The basis for different sensitivities of photosynthesis to SO2 in two cultivars of pea. J Exp Bot 38: 99–108 (1987).

    Google Scholar 

  3. Asada K, Takahashi M: Production and scavenging of active oxygen in photosynthesis. In: Kyle DJ, Osmond CB, Arntzen CJ (eds) Photoinhibition, pp. 227–287. Elsevier Science Publishers, Amsterdam (1987).

    Google Scholar 

  4. Beauchamp C, Fridovich I: Superoxide dismutase: improved assays and assays applicable to acrylamide gels. Anal Biochem 44: 276–287 (1971).

    Google Scholar 

  5. Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248–254 (1976).

    Google Scholar 

  6. Butler W, Cook L, Vayada ME: Hypoxic stress inhibits multiple aspects of the potato tuber wound response. Plant Physiol 93: 264–270 (1990).

    Google Scholar 

  7. Crosby JS, Vayada ME: Stress-induced translational control in potato tubers may be mediated by polysome-associated proteins. Plant Cell 3: 1013–1023 (1991).

    Google Scholar 

  8. Dhindsa RS, Plumb-Dhindsa P, Thorpe TA: Leaf senescence: correlated with increased levels of membrane permeability and lipid peroxidation, and decreased levels of superoxide dismutase and catalase. J Exp Bot 32: 93–101 (1981).

    Google Scholar 

  9. Droillard M, Paulin A: Isozymes of superoxide dismutase in mitochondria and peroxisomes isolates from petals of carnation (Dianthus caryophyllus) during senescence. Plant Physiol 94: 1187–1192 (1990).

    Google Scholar 

  10. Duke MV, Salin ML: Isozymes of cuprozinc superoxide dismutase from Pisum sativum. Phytochemistry 22: 2369–2373 (1983).

    Google Scholar 

  11. Foyer CH, Halliwell B: Presence of glutathione and glutathione reductase in chloroplasts: A proposed role in ascorbic acid metabolism. Planta 133: 21–25 (1976).

    Google Scholar 

  12. Furusawa I, Tanaka K, Thanutong P, Mizuguchi A, Yazaki M, Asada K: Paraquat resistant tobacco calluses with enhanced superoxide dismutase activity. Plant Cell Physiol 25: 1247–1254 (1984).

    Google Scholar 

  13. Grabau E: Nucleotide sequence of the soybean mitochondrial 18S rRNA gene: evidence for a slow rate of divergence in the plant mitochondrial genome. Plant Mol Biol 5: 119–124 (1985).

    Google Scholar 

  14. Hassan HM, Scandalios JG: Superoxide dismutases in aerobic organisms. In: Alscher RG, Cumming JR (eds) Stress Responses in Plants: Adaptation and Acclimation Mechanisms, pp. 175–199. Wiley-Liss, New York (1990).

    Google Scholar 

  15. Isin SH, Burke JJ, Allen RD: Sequence divergence of pea Cu/Zn superoxide dismutase II cDNAs. Plant Mol Biol 15: 789–791 (1990).

    Google Scholar 

  16. Kwiatowski J, Safianowska A, Kaniuga Z: Isolation and characterization of an iron-containing superoxide dismutase from tomato leaves, Lycopersicon esculentum. Eur J Biochem 146: 459–466 (1985).

    Google Scholar 

  17. Madamanchi NR, Alscher RG: Metabolic bases for differences in sensitivity of two pea cultivars to sulfur dioxide. Plant Physiol 97: 88–93 (1991).

    Google Scholar 

  18. Matters GL, Scandalios JG: Effect of the free radicalgenerating herbicide paraquat on the expression of the superoxide dismutase (SOD) genes in maize. Biochim Biophys Acta 882: 29–38 (1986).

    Google Scholar 

  19. Nakano Y, Asada K: Hydrogen peroxide is scavenged by ascorbate-specific peroxidase in spinach chloroplasts. Plant Cell Physiol 22: 867–880 (1981).

    Google Scholar 

  20. Perl-Treves R, Galun E: The tomato Cu,Zn superoxide dismutase genes are developmentally regulated and respond to light and stress. Plant Mol Biol 17: 745–760 (1991).

    Google Scholar 

  21. Pitcher LH, Altomare DA, Mittler R, Brennan E, Zilinskas BA: Molecular response of enzymatic antioxidants to ozone exposure. Abstract. The Third International Symposium on Gaseous Pollutants and Plant Metabolism, Blacksburg, VA (1992).

  22. Rabinowitch HD, Fridovich I: Dual Protection by superoxide dismutase in Chlorella sorokiniana. In: Cohen G, Greenwald RA (eds) Oxy Radicals and Their Scavenger Systems, vol I: Molecular aspects, pp. 222–227, Elsevier, New York (1983).

    Google Scholar 

  23. Rogers SO, Bendich AJ: Extraction of DNA from plant tissues. Gene Res Manual 1: 1–6 (1986).

    Google Scholar 

  24. Sambrook J, Fritsch T, Maniatis F: Molecular Cloning: A Laboratory Manual, 2nd ed. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY (1989).

    Google Scholar 

  25. Scioli JR, Zilinskas BA: Cloning and characterization of a cDNA encoding the chloroplastic copper/zinc-superoxide dismutase from pea. Proc Natl Acad Sci USA 85: 7661–7665 (1988).

    Google Scholar 

  26. Sevilla F, Lopez-Gorge J, Gomez M, Del Rio LA: Manganese superoxide dismutase from a higher plant. Planta 150: 153–157 (1980).

    Google Scholar 

  27. Shaaltiel Y, Glazer A, Bocion PF, Gressel J: Cross tolerance to herbicidal and environmental oxidants of plant biotypes tolerant to paraquat, sulfur dioxide, and ozone. Pestic Biochem Physiol 31: 13–23. (1988).

    Google Scholar 

  28. Shimazaki K, Sakaki T, Kondo N, Sugahara K: Active oxygen participation in chlorophyll destruction and lipid peroxidation in SO2-fumigated leaves of spinach. Plant Cell Physiol 21: 1193–1204 (1980).

    Google Scholar 

  29. Tanaka K, Sugahara K: Role of superoxide dismutase in defense against SO2 toxicity and an increase in superoxide dismutase activity with SO2 fumigation. Plant Cell Physiol 21: 601–611 (1980).

    Google Scholar 

  30. Tepperman JM, Dunsmuir P: Transformed plants with elevated levels of chloroplastic SOD are not more resistant to superoxide toxicity. Plant Mol Biol 14: 501–511 (1990).

    Google Scholar 

  31. Tsang EWT, Bowler C, Hérouart D, Camp WV, Villarroel R, Genetello C, Van Montagu MV, Inzé D: Differential regulation of superoxide dismutases in plants exposed to environmental stress. Plant Cell 3: 783–792 (1991).

    Google Scholar 

  32. White DA, Zilinskas BA: Nucleotide sequence of a complementary DNA encoding pea cytosolic copper/zinc superoxide dismutase. Plant Physiol 96: 1391–1392 (1991).

    Google Scholar 

  33. Wong-Vega L, Burke JJ, Allen RD: Isolation and sequence analysis of a cDNA that encodes pea manganese superoxide dismutase. Plant Mol Biol 17: 1271–1274 (1991).

    Google Scholar 

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Authors and Affiliations

  1. Department of Plant Pathology, Physiology and Weed Science, Virginia Polytechnic Institute and State University, 24061, Blacksburg, VA, USA

    Nageswara R. Madamanchi, Janet L. Donahue, Carole L. Cramer & Ruth G. Alscher

  2. Agricultural Biotechnology Program, Plant Molecular Biology Laboratory NLVF, NLH, 1432, Ås, Norway

    Karl Pedersen

Authors
  1. Nageswara R. Madamanchi
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  2. Janet L. Donahue
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  3. Carole L. Cramer
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  4. Ruth G. Alscher
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  5. Karl Pedersen
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Madamanchi, N.R., Donahue, J.L., Cramer, C.L. et al. Differential response of Cu,Zn superoxide dismutases in two pea cultivars during a short-term exposure to sulfur dioxide. Plant Mol Biol 26, 95–103 (1994). https://doi.org/10.1007/BF00039523

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  • DOI: https://doi.org/10.1007/BF00039523

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