Skip to main content
PMC home page
Plant Physiology logoLink to Plant Physiology
. 1997 Aug;114(4):1187–1196. doi: 10.1104/pp.114.4.1187

Characterization of Antisense Transformed Plants Deficient in the Tobacco Anionic Peroxidase.

L M Lagrimini 1, V Gingas 1, F Finger 1, S Rothstein 1, TTY Liu 1
PMCID: PMC158411  PMID: 12223765

Abstract

On the basis of the biological compounds that they metabolize, plant peroxidases have long been implicated in plant growth, cell wall biogenesis, lignification, and host defenses. Transgenic tobacco (Nicotiana tabacum L.) plants that underexpress anionic peroxidase were generated using antisense RNA. The antisense RNA was found to be specific for the anionic isoenzyme and highly effective, reducing endogenous transcript levels and total peroxidase activity by as much as 1600-fold. Antisense-transformed plants appeared normal at initial observation; however, growth studies showed that plants with reduced peroxidase activity grow taller and flower sooner than control plants. In contrast, previously transformed plants overproducing anionic peroxidase were shorter and flowered later than controls. Axillary buds were more developed in antisense-transformed plants and less developed in plants overproducing this enzyme. It was found that the lignin content in leaf, stem, and root was unchanged in antisense-transformed plants, which does not support a role for anionic peroxidase in the lignification of secondary xylem vessels. However, studies of wounded tissue show some reduction in wound-induced deposition of lignin-like polymers. The data support a possible role for tobacco anionic peroxidase in host defenses but not without a reduction in growth potential.

Full Text

The Full Text of this article is available as a PDF (2.5 MB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  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. Beffa R. S., Hofer R. M., Thomas M., Meins F., Jr Decreased Susceptibility to Viral Disease of [beta]-1,3-Glucanase-Deficient Plants Generated by Antisense Transformation. Plant Cell. 1996 Jun;8(6):1001–1011. doi: 10.1105/tpc.8.6.1001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Bruce R. J., West C. A. Elicitation of lignin biosynthesis and isoperoxidase activity by pectic fragments in suspension cultures of castor bean. Plant Physiol. 1989 Nov;91(3):889–897. doi: 10.1104/pp.91.3.889. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Epstein E., Cohen J. D., Bandurski R. S. Concentration and Metabolic Turnover of Indoles in Germinating Kernels of Zea mays L. Plant Physiol. 1980 Mar;65(3):415–421. doi: 10.1104/pp.65.3.415. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Gazaryan I. G., Lagrimini L. M., Ashby G. A., Thorneley R. N. Mechanism of indole-3-acetic acid oxidation by plant peroxidases: anaerobic stopped-flow spectrophotometric studies on horseradish and tobacco peroxidases. Biochem J. 1996 Feb 1;313(Pt 3):841–847. doi: 10.1042/bj3130841. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Harkin J. M., Obst J. R. Lignification in trees: indication of exclusive peroxidase participation. Science. 1973 Apr 20;180(4083):296–298. doi: 10.1126/science.180.4083.296. [DOI] [PubMed] [Google Scholar]
  7. Hewelt A., Prinsen E., Schell J., Van Onckelen H., Schmülling T. Promoter tagging with a promoterless ipt gene leads to cytokinin-induced phenotypic variability in transgenic tobacco plants:implications of gene dosage effects. Plant J. 1994 Dec;6(6):879–891. doi: 10.1046/j.1365-313x.1994.6060879.x. [DOI] [PubMed] [Google Scholar]
  8. Jiang C. Z., Rodermel S. R. Regulation of Photosynthesis during Leaf Development in RbcS Antisense DNA Mutants of Tobacco. Plant Physiol. 1995 Jan;107(1):215–224. doi: 10.1104/pp.107.1.215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Kirk T. K., Connors W. J., Bleam R. D., Hackett W. F., Zeikus J. G. Preparation and microbial decomposition of synthetic [14C]ligins. Proc Natl Acad Sci U S A. 1975 Jul;72(7):2515–2519. doi: 10.1073/pnas.72.7.2515. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Kuipers A. G., Soppe W. J., Jacobsen E., Visser R. G. Factors affecting the inhibition by antisense RNA of granule-bound starch synthase gene expression in potato. Mol Gen Genet. 1995 Mar 20;246(6):745–755. doi: 10.1007/BF00290722. [DOI] [PubMed] [Google Scholar]
  11. Lagrimini L. M., Burkhart W., Moyer M., Rothstein S. Molecular cloning of complementary DNA encoding the lignin-forming peroxidase from tobacco: Molecular analysis and tissue-specific expression. Proc Natl Acad Sci U S A. 1987 Nov;84(21):7542–7546. doi: 10.1073/pnas.84.21.7542. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Lagrimini L. M., Joly R. J., Dunlap J. R., Liu T. T. The consequence of peroxidase overexpression in transgenic plants on root growth and development. Plant Mol Biol. 1997 Mar;33(5):887–895. doi: 10.1023/a:1005756713493. [DOI] [PubMed] [Google Scholar]
  13. 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]
  14. Lagrimini L. M. Wound-induced deposition of polyphenols in transgenic plants overexpressing peroxidase. Plant Physiol. 1991 Jun;96(2):577–583. doi: 10.1104/pp.96.2.577. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. 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]
  16. 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]
  17. Rodermel S. R., Abbott M. S., Bogorad L. Nuclear-organelle interactions: nuclear antisense gene inhibits ribulose bisphosphate carboxylase enzyme levels in transformed tobacco plants. Cell. 1988 Nov 18;55(4):673–681. doi: 10.1016/0092-8674(88)90226-7. [DOI] [PubMed] [Google Scholar]
  18. Romano C. P., Hein M. B., Klee H. J. Inactivation of auxin in tobacco transformed with the indoleacetic acid-lysine synthetase gene of Pseudomonas savastanoi. Genes Dev. 1991 Mar;5(3):438–446. doi: 10.1101/gad.5.3.438. [DOI] [PubMed] [Google Scholar]
  19. 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]
  20. Sherf B. A., Bajar A. M., Kolattukudy P. E. Abolition of an Inducible Highly Anionic Peroxidase Activity in Transgenic Tomato. Plant Physiol. 1993 Jan;101(1):201–208. doi: 10.1104/pp.101.1.201. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Tenhaken R., Levine A., Brisson L. F., Dixon R. A., Lamb C. Function of the oxidative burst in hypersensitive disease resistance. Proc Natl Acad Sci U S A. 1995 May 9;92(10):4158–4163. doi: 10.1073/pnas.92.10.4158. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Teutonico R. A., Dudley M. W., Orr J. D., Lynn D. G., Binns A. N. Activity and accumulation of cell division-promoting phenolics in tobacco tissue cultures. Plant Physiol. 1991 Sep;97(1):288–297. doi: 10.1104/pp.97.1.288. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Ward E. R., Uknes S. J., Williams S. C., Dincher S. S., Wiederhold D. L., Alexander D. C., Ahl-Goy P., Metraux J. P., Ryals J. A. Coordinate Gene Activity in Response to Agents That Induce Systemic Acquired Resistance. Plant Cell. 1991 Oct;3(10):1085–1094. doi: 10.1105/tpc.3.10.1085. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES