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Plant Physiology 64:38-42 (1979)
© 1979 American Society of Plant Biologists

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Articles

Rapid Degradation and Limited Synthesis of Phospholipids in the Cotyledons of Mung Bean Seedlings 1

Neil R. Gilkes, Eliot M. Herman and Maarten J. Chrispeels2

a Department of Biology, C-016, University of California/San Diego, La Jolla, California 92093

Seedling growth of mung bean is accompanied by the rapid catabolism of the three major phospholipids in the cotyledons (phosphatidylcholine, phosphatidylethanolamine, and phosphatidylinositol). The decline starts 24 hours after the beginning of imbibition and by the 4th day of growth more than 50% of the phospholipids have been catabolized. Extracts of cotyledons of 24-hour-imbibed beans contain enzymes capable of degrading membrane-associated phospholipids in vitro. This degradation involves phospholipase D and phosphatase activity.

Studies with radioactive acetate, glycerol, and orthophosphate indicate that the three major phospholipids are also synthesized in the cotyledons. Incorporation of glycerol and acetate into phospholipids of cotyledons is relatively constant throughout seedling growth, while the incorporation of [32P]orthophosphate steadily declines from a high value 24 hours after the start of imbibition. The newly synthesized phospholipids become associated with membranous organelles, especially the endoplasmic reticulum, and have an in situ half-life of 2 to 2.5 days.

Determination of the activities of two enzymes involved in phospholipid biosynthesis (phosphorylcholine-glyceride transferase and CDP-diglyceride-inositol transferase) shows that the enzymes have their highest activities 12 hours after the start of imbibition. High activities for both enzymes were found in cotyledons of beans incubated at 1 C, indicating that the enzymes may preexist in the dry seeds.

The experiments demonstrate that cotyledons start synthesizing new phospholipids immediately after imbibition, but that the rate of phospholipid catabolism far exceeds the rate of synthesis long before the cotyledons start to senesce.


2 To whom inquiries should be addressed.

1 This research has been supported by a grant from the National Science Foundation (Metabolic Biology).




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E. Herman and M. Schmidt
Endoplasmic Reticulum to Vacuole Trafficking of Endoplasmic Reticulum Bodies Provides an Alternate Pathway for Protein Transfer to the Vacuole
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A. J. Kinney, R. Jung, and E. M. Herman
Cosuppression of the {{alpha}} Subunits of {beta}-Conglycinin in Transgenic Soybean Seeds Induces the Formation of Endoplasmic Reticulum-Derived Protein Bodies
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