Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1996 Jan;110(1):287–299. doi: 10.1104/pp.110.1.287

The differential expression of wound-inducible lipoxygenase genes in soybean leaves.

D M Saravitz 1, J N Siedow 1
PMCID: PMC157720  PMID: 8587989

Abstract

Two soybean [Glycine max (L.) Merr.] lipoxygenase cDNA clones were isolated that represent lipoxygenase genes (designated LOX7 and LOX8) that display increased expression in leaves following wounding. LOX7 and LOX8 were found to be differentially expressed in soybean leaves after wounding. Increased transcript levels of both genes were detected in wounded leaves within 8 h after wounding, but only the expression of LOX7 displayed a systemic wound response. Additionally, the elevated expression of LOX7 in wounded leaves was transient. Twenty-four hours postwounding, LOX7 transcripts were no longer detectable in leaves. In contrast, LOX8 transcript levels were elevated in wounded leaves from 8 to 72 h after wounding. In addition, treatment of soybean plants with methyl jasmonate resulted in higher levels of both LOX7 and LOX8 transcripts in leaves. High levels of expression of both genes were also detected in young leaves, flowers, and immature seed pods, and increases in LOX7 and LOX8 transcripts were observed in leaves following the removal of reproductive sink tissues. The expression of LOX7 and LOX8 in unwounded soybean tissues and increased expression following wounding suggest that the lipoxygenases encoded by these genes may participate in general physiological processes that are enhanced following physical damage.

Full Text

The Full Text of this article is available as a PDF (4.1 MB).

Selected References

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

  1. Bell E., Mullet J. E. Characterization of an Arabidopsis lipoxygenase gene responsive to methyl jasmonate and wounding. Plant Physiol. 1993 Dec;103(4):1133–1137. doi: 10.1104/pp.103.4.1133. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bell E., Mullet J. E. Lipoxygenase gene expression is modulated in plants by water deficit, wounding, and methyl jasmonate. Mol Gen Genet. 1991 Dec;230(3):456–462. doi: 10.1007/BF00280303. [DOI] [PubMed] [Google Scholar]
  3. Bunker T. W., Koetje D. S., Stephenson L. C., Creelman R. A., Mullet J. E., Grimes H. D. Sink limitation induces the expression of multiple soybean vegetative lipoxygenase mRNAs while the endogenous jasmonic acid level remains low. Plant Cell. 1995 Aug;7(8):1319–1331. doi: 10.1105/tpc.7.8.1319. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Casey J., Davidson N. Rates of formation and thermal stabilities of RNA:DNA and DNA:DNA duplexes at high concentrations of formamide. Nucleic Acids Res. 1977;4(5):1539–1552. doi: 10.1093/nar/4.5.1539. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Conkling M. A., Cheng C. L., Yamamoto Y. T., Goodman H. M. Isolation of transcriptionally regulated root-specific genes from tobacco. Plant Physiol. 1990 Jul;93(3):1203–1211. doi: 10.1104/pp.93.3.1203. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Creelman R. A., Tierney M. L., Mullet J. E. Jasmonic acid/methyl jasmonate accumulate in wounded soybean hypocotyls and modulate wound gene expression. Proc Natl Acad Sci U S A. 1992 Jun 1;89(11):4938–4941. doi: 10.1073/pnas.89.11.4938. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Croft KPC., Juttner F., Slusarenko A. J. Volatile Products of the Lipoxygenase Pathway Evolved from Phaseolus vulgaris (L.) Leaves Inoculated with Pseudomonas syringae pv phaseolicola. Plant Physiol. 1993 Jan;101(1):13–24. doi: 10.1104/pp.101.1.13. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Farmer E. E., Johnson R. R., Ryan C. A. Regulation of expression of proteinase inhibitor genes by methyl jasmonate and jasmonic Acid. Plant Physiol. 1992 Mar;98(3):995–1002. doi: 10.1104/pp.98.3.995. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Farmer E. E., Ryan C. A. Octadecanoid Precursors of Jasmonic Acid Activate the Synthesis of Wound-Inducible Proteinase Inhibitors. Plant Cell. 1992 Feb;4(2):129–134. doi: 10.1105/tpc.4.2.129. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Franceschi V. R., Wittenbach V. A., Giaquinta R. T. Paraveinal Mesophyll of Soybean Leaves in Relation to Assimilate Transfer and Compartmentation : III. Immunohistochemical Localization of Specific Glycopeptides in the Vacuole after Depodding. Plant Physiol. 1983 Jun;72(2):586–589. doi: 10.1104/pp.72.2.586. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Grimes H. D., Koetje D. S., Franceschi V. R. Expression, activity, and cellular accumulation of methyl jasmonate-responsive lipoxygenase in soybean seedlings. Plant Physiol. 1992 Sep;100(1):433–443. doi: 10.1104/pp.100.1.433. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Grimes H. D., Tranbarger T. J., Franceschi V. R. Expression and Accumulation Patterns of Nitrogen-Responsive Lipoxygenase in Soybeans. Plant Physiol. 1993 Oct;103(2):457–466. doi: 10.1104/pp.103.2.457. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Gundlach H., Müller M. J., Kutchan T. M., Zenk M. H. Jasmonic acid is a signal transducer in elicitor-induced plant cell cultures. Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2389–2393. doi: 10.1073/pnas.89.6.2389. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Johnson R., Narvaez J., An G., Ryan C. Expression of proteinase inhibitors I and II in transgenic tobacco plants: effects on natural defense against Manduca sexta larvae. Proc Natl Acad Sci U S A. 1989 Dec;86(24):9871–9875. doi: 10.1073/pnas.86.24.9871. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Kauss H., Krause K., Jeblick W. Methyl jasmonate conditions parsley suspension cells for increased elicitation of phenylpropanoid defense responses. Biochem Biophys Res Commun. 1992 Nov 30;189(1):304–308. doi: 10.1016/0006-291x(92)91558-8. [DOI] [PubMed] [Google Scholar]
  16. Koch E., Meier B. M., Eiben H. G., Slusarenko A. A Lipoxygenase from Leaves of Tomato (Lycopersicon esculentum Mill.) Is Induced in Response to Plant Pathogenic Pseudomonads. Plant Physiol. 1992 Jun;99(2):571–576. doi: 10.1104/pp.99.2.571. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Koda Y. The role of jasmonic acid and related compounds in the regulation of plant development. Int Rev Cytol. 1992;135:155–199. doi: 10.1016/s0074-7696(08)62040-9. [DOI] [PubMed] [Google Scholar]
  18. Melan M. A., Dong X., Endara M. E., Davis K. R., Ausubel F. M., Peterman T. K. An Arabidopsis thaliana lipoxygenase gene can be induced by pathogens, abscisic acid, and methyl jasmonate. Plant Physiol. 1993 Feb;101(2):441–450. doi: 10.1104/pp.101.2.441. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Ohta H., Shida K., Peng Y. L., Furusawa I., Shishiyama J., Aibara S., Morita Y. A Lipoxygenase Pathway Is Activated in Rice after Infection with the Rice Blast Fungus Magnaporthe grisea. Plant Physiol. 1991 Sep;97(1):94–98. doi: 10.1104/pp.97.1.94. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Rouzer C. A., Matsumoto T., Samuelsson B. Single protein from human leukocytes possesses 5-lipoxygenase and leukotriene A4 synthase activities. Proc Natl Acad Sci U S A. 1986 Feb;83(4):857–861. doi: 10.1073/pnas.83.4.857. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Ryan C. A. The search for the proteinase inhibitor-inducing factor, PIIF. Plant Mol Biol. 1992 May;19(1):123–133. doi: 10.1007/BF00015610. [DOI] [PubMed] [Google Scholar]
  22. Samuelsson B., Dahlén S. E., Lindgren J. A., Rouzer C. A., Serhan C. N. Leukotrienes and lipoxins: structures, biosynthesis, and biological effects. Science. 1987 Sep 4;237(4819):1171–1176. doi: 10.1126/science.2820055. [DOI] [PubMed] [Google Scholar]
  23. Samuelsson B. Leukotrienes: mediators of immediate hypersensitivity reactions and inflammation. Science. 1983 May 6;220(4597):568–575. doi: 10.1126/science.6301011. [DOI] [PubMed] [Google Scholar]
  24. Saravitz D. M., Siedow J. N. The Lipoxygenase Isozymes in Soybean [Glycine max (L.) Merr.] Leaves (Changes during Leaf Development, after Wounding, and following Reproductive Sink Removal). Plant Physiol. 1995 Feb;107(2):535–543. doi: 10.1104/pp.107.2.535. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Setter T. L., Brun W. A., Brenner M. L. Effect of obstructed translocation on leaf abscisic Acid, and associated stomatal closure and photosynthesis decline. Plant Physiol. 1980 Jun;65(6):1111–1115. doi: 10.1104/pp.65.6.1111. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Shibata D., Kato T., Tanaka K. Nucleotide sequences of a soybean lipoxygenase gene and the short intergenic region between an upstream lipoxygenase gene. Plant Mol Biol. 1991 Feb;16(2):353–359. doi: 10.1007/BF00020569. [DOI] [PubMed] [Google Scholar]
  27. Shibata D., Steczko J., Dixon J. E., Andrews P. C., Hermodson M., Axelrod B. Primary structure of soybean lipoxygenase L-2. J Biol Chem. 1988 May 15;263(14):6816–6821. [PubMed] [Google Scholar]
  28. Shibata D., Steczko J., Dixon J. E., Hermodson M., Yazdanparast R., Axelrod B. Primary structure of soybean lipoxygenase-1. J Biol Chem. 1987 Jul 25;262(21):10080–10085. [PubMed] [Google Scholar]
  29. Steczko J., Donoho G. P., Clemens J. C., Dixon J. E., Axelrod B. Conserved histidine residues in soybean lipoxygenase: functional consequences of their replacement. Biochemistry. 1992 Apr 28;31(16):4053–4057. doi: 10.1021/bi00131a022. [DOI] [PubMed] [Google Scholar]
  30. Tranbarger T. J., Franceschi V. R., Hildebrand D. F., Grimes H. D. The soybean 94-kilodalton vegetative storage protein is a lipoxygenase that is localized in paraveinal mesophyll cell vacuoles. Plant Cell. 1991 Sep;3(9):973–987. doi: 10.1105/tpc.3.9.973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Wittenbach V. A. Effect of pod removal on leaf senescence in soybeans. Plant Physiol. 1982 Nov;70(5):1544–1548. doi: 10.1104/pp.70.5.1544. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Wolfe L. S. Eicosanoids: prostaglandins, thromboxanes, leukotrienes, and other derivatives of carbon-20 unsaturated fatty acids. J Neurochem. 1982 Jan;38(1):1–14. doi: 10.1111/j.1471-4159.1982.tb10847.x. [DOI] [PubMed] [Google Scholar]

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

RESOURCES