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. 1992 Mar;98(3):995–1002. doi: 10.1104/pp.98.3.995

Regulation of Expression of Proteinase Inhibitor Genes by Methyl Jasmonate and Jasmonic Acid 1

Edward E Farmer 1, Russell R Johnson 1,2, Clarence A Ryan 1
PMCID: PMC1080300  PMID: 16668777

Abstract

Gel electrophoretic analysis of the proteinase inhibitor proteins induced in tomato leaves by airborne methyl jasmonate (EE Farmer, CA Ryan [1990] Proc Natl Acad Sci USA 87: 7713-7716) revealed the new appearance of inhibitors I and II and two other, higher molecular mass proteins (63.5 and 87 kilodaltons). Northern analysis of methyl jasmonate-induced inhibitors I and II mRNAs in tomato (Lycopersicon esculentum) leaves, and of alfalfa trypsin inhibitor (a Bowman-Birk family inhibitor) mRNA in alfalfa (Medicago sativa) leaves, indicated that nascent inhibitor mRNAs were regulated in a manner similar to wounding, that is, at the transcriptional level. In tobacco (Nicotiana tabacum), transformed with a fused gene composed of the 5′ and 3′ regions of a wound-inducible potato inhibitor II and a chloramphenicol acetyl transferase (CAT) gene coding region, CAT activity was induced in leaves by methyl jasmonate, consistent with a transcriptional regulation of the inhibitor II gene. In tomato leaves, inhibitor I and II mRNAs and proteins accumulated in leaves distal to those exposed to methyl jasmonate or jasmonic acid to similar levels as in exposed leaves. We suggest that in response to wound signals generated by insect or pathogen attacks, linolenic acid is released into the cytoplasm from plant cell membrane lipids and is rapidly converted in cells to jasmonic acid (or perhaps a closely related derivative such as methyl jasmonate), which serves as a signal to regulate the expression of proteinase inhibitor genes.

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Selected References

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  1. Brown W. E., Ryan C. A. Isolation and characterization of a wound-induced trypsin inhibitor from alfalfa leaves. Biochemistry. 1984 Jul 17;23(15):3418–3422. doi: 10.1021/bi00310a006. [DOI] [PubMed] [Google Scholar]
  2. 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]
  3. Graham J. S., Pearce G., Merryweather J., Titani K., Ericsson L. H., Ryan C. A. Wound-induced proteinase inhibitors from tomato leaves. II. The cDNA-deduced primary structure of pre-inhibitor II. J Biol Chem. 1985 Jun 10;260(11):6561–6564. [PubMed] [Google Scholar]
  4. Graham J. S., Pearce G., Merryweather J., Titani K., Ericsson L., Ryan C. A. Wound-induced proteinase inhibitors from tomato leaves. I. The cDNA-deduced primary structure of pre-inhibitor I and its post-translational processing. J Biol Chem. 1985 Jun 10;260(11):6555–6560. [PubMed] [Google Scholar]
  5. Green T. R., Ryan C. A. Wound-Induced Proteinase Inhibitor in Plant Leaves: A Possible Defense Mechanism against Insects. Science. 1972 Feb 18;175(4023):776–777. doi: 10.1126/science.175.4023.776. [DOI] [PubMed] [Google Scholar]
  6. 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]
  7. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  8. Lawton M. A., Dixon R. A., Hahlbrock K., Lamb C. J. Elicitor induction of mRNA activity. Rapid effects of elicitor on phenylalanine ammonia-lyase and chalcone synthase mRNA activities in bean cells. Eur J Biochem. 1983 Jan 17;130(1):131–139. [PubMed] [Google Scholar]
  9. Mason H. S., Mullet J. E. Expression of two soybean vegetative storage protein genes during development and in response to water deficit, wounding, and jasmonic acid. Plant Cell. 1990 Jun;2(6):569–579. doi: 10.1105/tpc.2.6.569. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Pautot V., Holzer F. M., Walling L. L. Differential expression of tomato proteinase inhibitor I and II genes during bacterial pathogen invasion and wounding. Mol Plant Microbe Interact. 1991 May-Jun;4(3):284–292. doi: 10.1094/mpmi-4-284. [DOI] [PubMed] [Google Scholar]
  11. Pearce G., Strydom D., Johnson S., Ryan C. A. A polypeptide from tomato leaves induces wound-inducible proteinase inhibitor proteins. Science. 1991 Aug 23;253(5022):895–897. doi: 10.1126/science.253.5022.895. [DOI] [PubMed] [Google Scholar]
  12. Ryan C. A. Quantitative determination of soluble cellular proteins by radial diffusion in agar gels containing antibodies. Anal Biochem. 1967 Jun;19(3):434–440. doi: 10.1016/0003-2697(67)90233-3. [DOI] [PubMed] [Google Scholar]
  13. Staswick P. E. Novel Regulation of Vegetative Storage Protein Genes. Plant Cell. 1990 Jan;2(1):1–6. doi: 10.1105/tpc.2.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Swank R. T., Munkres K. D. Molecular weight analysis of oligopeptides by electrophoresis in polyacrylamide gel with sodium dodecyl sulfate. Anal Biochem. 1971 Feb;39(2):462–477. doi: 10.1016/0003-2697(71)90436-2. [DOI] [PubMed] [Google Scholar]
  15. Thornburg R. W., An G., Cleveland T. E., Johnson R., Ryan C. A. Wound-inducible expression of a potato inhibitor II-chloramphenicol acetyltransferase gene fusion in transgenic tobacco plants. Proc Natl Acad Sci U S A. 1987 Feb;84(3):744–748. doi: 10.1073/pnas.84.3.744. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Trautman R., Cowan K. M., Wagner G. G. Data processing for radial immunodiffusion. Immunochemistry. 1971 Oct;8(10):901–916. doi: 10.1016/0019-2791(71)90429-0. [DOI] [PubMed] [Google Scholar]
  17. Vick B. A., Zimmerman D. C. Biosynthesis of jasmonic Acid by several plant species. Plant Physiol. 1984 Jun;75(2):458–461. doi: 10.1104/pp.75.2.458. [DOI] [PMC free article] [PubMed] [Google Scholar]

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