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. 1990 Jan;2(1):7–18. doi: 10.1105/tpc.2.1.7

Peroxidase-Induced Wilting in Transgenic Tobacco Plants.

LM Lagrimini 1, S Bradford 1, S Rothstein 1
PMCID: PMC159859  PMID: 12354942

Abstract

Peroxidases are a family of isoenzymes found in all higher plants. However, little is known concerning their role in growth, development, or response to stress. Plant peroxidases are heme-containing monomeric glycoproteins that utilize either H2O2 or O2 to oxidize a wide variety of molecules. To obtain more information on possible in planta functions of peroxidases, we have used a cDNA clone for the primary isoenzyme form of peroxidase to synthesize high levels of this enzyme in transgenic plants. We were able to obtain Nicotiana tabacum and N. sylvestris transformed plants with peroxidase activity that is 10-fold higher than in wild-type plants by introducing a chimeric gene composed of the cauliflower mosaic virus 35S promoter and the tobacco anionic peroxidase cDNA. The elevated peroxidase activity was a result of increased levels of two anionic peroxidases in N. tabacum, which apparently differ in post-translational modification. Transformed plants of both species have the unique phenotype of chronic severe wilting through loss of turgor in leaves, which was initiated at the time of flowering. The peroxidase-induced wilting was shown not to be an effect of diminished water uptake through the roots, decreased conductance of water through the xylem, or increased water loss through the leaf surface or stomata. Possible explanations for the loss of turgor, and the significance of these types of experiments in studying isoenzyme families, are discussed.

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Selected References

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  1. A simple and general method for transferring genes into plants. Science. 1985 Mar 8;227(4691):1229–1231. doi: 10.1126/science.227.4691.1229. [DOI] [PubMed] [Google Scholar]
  2. Espelie K. E., Franceschi V. R., Kolattukudy P. E. Immunocytochemical localization and time course of appearance of an anionic peroxidase associated with suberization in wound-healing potato tuber tissue. Plant Physiol. 1986 Jun;81(2):487–492. doi: 10.1104/pp.81.2.487. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Fischer R. A. Stomatal Opening in Isolated Epidermal Strips of Vicia faba. I. Response to Light and to CO(2)-free Air. Plant Physiol. 1968 Dec;43(12):1947–1952. doi: 10.1104/pp.43.12.1947. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. HINMAN R. L., LANG J. PEROXIDASE-CATALYZED OXIDATION OF INDOLE-3-ACETIC ACID. Biochemistry. 1965 Jan;4:144–158. doi: 10.1021/bi00877a023. [DOI] [PubMed] [Google Scholar]
  5. Jefferson R. A., Kavanagh T. A., Bevan M. W. GUS fusions: beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J. 1987 Dec 20;6(13):3901–3907. doi: 10.1002/j.1460-2075.1987.tb02730.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Lagrimini L. M., Rothstein S. Tissue specificity of tobacco peroxidase isozymes and their induction by wounding and tobacco mosaic virus infection. Plant Physiol. 1987 Jun;84(2):438–442. doi: 10.1104/pp.84.2.438. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Lehrach H., Diamond D., Wozney J. M., Boedtker H. RNA molecular weight determinations by gel electrophoresis under denaturing conditions, a critical reexamination. Biochemistry. 1977 Oct 18;16(21):4743–4751. doi: 10.1021/bi00640a033. [DOI] [PubMed] [Google Scholar]
  8. Mäder M., Füssl R. Role of Peroxidase in Lignification of Tobacco Cells : II. Regulation by Phenolic Compounds. Plant Physiol. 1982 Oct;70(4):1132–1134. doi: 10.1104/pp.70.4.1132. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Rothstein S. J., Lahners K. N., Lotstein R. J., Carozzi N. B., Jayne S. M., Rice D. A. Promoter cassettes, antibiotic-resistance genes, and vectors for plant transformation. Gene. 1987;53(2-3):153–161. doi: 10.1016/0378-1119(87)90003-5. [DOI] [PubMed] [Google Scholar]
  10. Tal M. Abnormal stomatal behavior in wilty mutants of tomato. Plant Physiol. 1966 Oct;41(8):1387–1391. doi: 10.1104/pp.41.8.1387. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Tal M., Nevo Y. Abnormal stomatal behavior and root resistance, and hormonal imbalance in three wilty mutants of tomato. Biochem Genet. 1973 Mar;8(3):291–300. doi: 10.1007/BF00486182. [DOI] [PubMed] [Google Scholar]
  12. Thomas P. S. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc Natl Acad Sci U S A. 1980 Sep;77(9):5201–5205. doi: 10.1073/pnas.77.9.5201. [DOI] [PMC free article] [PubMed] [Google Scholar]

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