Skip to main content
PMC home page
Plant Physiology logoLink to Plant Physiology
. 1993 Dec;103(4):1211–1219. doi: 10.1104/pp.103.4.1211

Membrane-Associated and Soluble Lipoxygenase Isoforms in Tomato Pericarp (Characterization and Involvement in Membrane Alterations).

M J Droillard 1, M A Rouet-Mayer 1, J M Bureau 1, C Lauriere 1
PMCID: PMC159108  PMID: 12232014

Abstract

Membrane-associated and soluble lipoxygenases from green tomato (Lycopersicon esculentum Mill. cv Ailsa Craig) fruit have been identified. Microsomal lipoxygenase was localized partly in the plasma membrane and tonoplast fractions. The possibilities of glycosyl-phosphatidylinositol or transmembrane polypeptide anchors in the membrane were ruled out by differential solubilization and temperature-induced phase separation in Triton X-114. High performance liquid chromatography of reaction products combined with polarography showed that tomato lipoxygenase is capable of specific oxygenation of fatty acids esterified in phospholipids. This possibility of direct action on membrane phospholipids strengthened the hypothesis of a role for lipoxygenase in plant senescence and membrane turnover. Membrane-associated lipoxygenase is polymorphic, with two forms differing by their isoelectric points (pls) (around 4.2 and 5.1). The pl of the soluble lipoxygenase corresponds to the minor microsomal enzyme, with a pl of 5.1. The charge-differing isoforms were separated and analyzed by western blotting using anti-soybean lipoxygenase antibodies. A single polypeptide with an apparent molecular weight of 92,000 was identified in each case for the soluble and microsomal enzymes. It is suggested that a charge modification of the soluble lipoxygenase allows its association with the membrane.

Full Text

The Full Text of this article is available as a PDF (2.0 MB).

Selected References

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

  1. Augustine J. A., Secrist J. P., Daniels J. K., Leibson P. J., Abraham R. T. Signal transduction through the T cell antigen receptor. Activation of phospholipase C through a G protein-independent coupling mechanism. J Immunol. 1991 May 1;146(9):2889–2897. [PubMed] [Google Scholar]
  2. BLIGH E. G., DYER W. J. A rapid method of total lipid extraction and purification. Can J Biochem Physiol. 1959 Aug;37(8):911–917. doi: 10.1139/o59-099. [DOI] [PubMed] [Google Scholar]
  3. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
  4. Hooper N. M., Bashir A. Glycosyl-phosphatidylinositol-anchored membrane proteins can be distinguished from transmembrane polypeptide-anchored proteins by differential solubilization and temperature-induced phase separation in Triton X-114. Biochem J. 1991 Dec 15;280(Pt 3):745–751. doi: 10.1042/bj2800745. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Kuhn H., Belkner J., Wiesner R., Brash A. R. Oxygenation of biological membranes by the pure reticulocyte lipoxygenase. J Biol Chem. 1990 Oct 25;265(30):18351–18361. [PubMed] [Google Scholar]
  6. Laurière M., Laurière C., Chrispeels M. J., Johnson K. D., Sturm A. Characterization of a xylose-specific antiserum that reacts with the complex asparagine-linked glycans of extracellular and vacuolar glycoproteins. Plant Physiol. 1989 Jul;90(3):1182–1188. doi: 10.1104/pp.90.3.1182. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Murray J. J., Brash A. R. Rabbit reticulocyte lipoxygenase catalyzes specific 12(S) and 15(S) oxygenation of arachidonoyl-phosphatidylcholine. Arch Biochem Biophys. 1988 Sep;265(2):514–523. doi: 10.1016/0003-9861(88)90156-7. [DOI] [PubMed] [Google Scholar]
  8. Reddanna P., Whelan J., Reddy P. S., Reddy C. C. Isolation and characterization of 5-lipoxygenase from tulip bulbs. Biochem Biophys Res Commun. 1988 Dec 30;157(3):1348–1351. doi: 10.1016/s0006-291x(88)81023-4. [DOI] [PubMed] [Google Scholar]
  9. Rigaud M., Benit E., Castadot M., Lacombe P., Delorme G., Bardet J., Bourdarias J. P. Comparative effects of enoximone and nitroglycerin on left ventricular performance and regional wall motion in ischaemic cardiomyopathy. Br J Clin Pract Suppl. 1988 Dec;64:26–34. [PubMed] [Google Scholar]
  10. Schewe T., Rapoport S. M., Kühn H. Enzymology and physiology of reticulocyte lipoxygenase: comparison with other lipoxygenases. Adv Enzymol Relat Areas Mol Biol. 1986;58:191–272. doi: 10.1002/9780470123041.ch6. [DOI] [PubMed] [Google Scholar]
  11. Surrey K. Spectrophotometric Method for Determination of Lipoxidase Activity. Plant Physiol. 1964 Jan;39(1):65–70. doi: 10.1104/pp.39.1.65. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. 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]
  13. Verhue W. M., Francke A. The heterogeneity of soyabean lipoxygenase. Biochim Biophys Acta. 1972 Sep 19;284(1):43–53. doi: 10.1016/0005-2744(72)90044-7. [DOI] [PubMed] [Google Scholar]

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

RESOURCES