Skip to main content
Plant Physiology logoLink to Plant Physiology
. 1995 Dec;109(4):1227–1230. doi: 10.1104/pp.109.4.1227

Effect of volatile methyl jasmonate on the oxylipin pathway in tobacco, cucumber, and arabidopsis.

S Avdiushko 1, K P Croft 1, G C Brown 1, D M Jackson 1, T R Hamilton-Kemp 1, D Hildebrand 1
PMCID: PMC157654  PMID: 8539290

Abstract

The effect of atmospheric methyl jasmonate on the oxylipin pathway was investigated in leaves of tobacco (Nicotiana tabacum L.), cucumber (Cucumis sativa L.), and Arabidopsis thaliana (L.). Differential sensitivities of test plants to methyl jasmonate were observed. Thus, different concentrations of methyl jasmonate were required for induction of changes in the oxylipin pathway. Arabidopsis was the least and cucumber the most sensitive to methyl jasmonate. Methyl jasmonate induced the accumulation of lipoxygenase protein and a corresponding increase in extractable lipoxygenase activity. Atmospheric methyl jasmonate additionally induced hydroperoxide lyase activity and the enhanced production of several volatile six-carbon products. It is interesting that lipid hydroperoxidase activity, which is a measure of hydroperoxide lyase plus allene oxide synthase plus possibly other lipid hydroperoxide-metabolizing activities, was not changed by methyl jasmonate treatment. Methyl jasmonate selectively altered the activity of certain enzymes of the oxylipin pathway (lipoxygenase and hydroperoxide lyase) and increased the potential of leaves for greatly enhanced six-carbon-volatile production.

Full Text

The Full Text of this article is available as a PDF (970.7 KB).

Selected References

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

  1. Farmer E. E., Ryan C. A. Interplant communication: airborne methyl jasmonate induces synthesis of proteinase inhibitors in plant leaves. Proc Natl Acad Sci U S A. 1990 Oct;87(19):7713–7716. doi: 10.1073/pnas.87.19.7713. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. 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]
  3. Franceschi V. R., Grimes H. D. Induction of soybean vegetative storage proteins and anthocyanins by low-level atmospheric methyl jasmonate. Proc Natl Acad Sci U S A. 1991 Aug 1;88(15):6745–6749. doi: 10.1073/pnas.88.15.6745. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Grayburn W. S., Schneider G. R., Hamilton-Kemp T. R., Bookjans G., Ali K., Hildebrand D. F. Soybean leaves contain multiple lipoxygenases. Plant Physiol. 1991 Apr;95(4):1214–1218. doi: 10.1104/pp.95.4.1214. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. 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]
  6. Hamberg M., Gardner H. W. Oxylipin pathway to jasmonates: biochemistry and biological significance. Biochim Biophys Acta. 1992 Nov 11;1165(1):1–18. doi: 10.1016/0005-2760(92)90069-8. [DOI] [PubMed] [Google Scholar]
  7. 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]
  8. Reinbothe S., Mollenhauer B., Reinbothe C. JIPs and RIPs: the regulation of plant gene expression by jasmonates in response to environmental cues and pathogens. Plant Cell. 1994 Sep;6(9):1197–1209. doi: 10.1105/tpc.6.9.1197. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Song W. C., Brash A. R. Purification of an allene oxide synthase and identification of the enzyme as a cytochrome P-450. Science. 1991 Aug 16;253(5021):781–784. doi: 10.1126/science.1876834. [DOI] [PubMed] [Google Scholar]
  10. 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]

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

RESOURCES