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Plant Physiology 91:1275-1279 (1989)
© 1989 American Society of Plant Biologists

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Metabolism and Enzymology

Characterization of a Polyphosphoinositide Phospholipase C from the Plasma Membrane of Avena sativa1

Bonnie F. Tate, G. Eric Schaller, Michael R. Sussman and Richard C. Crain

Department of Molecular and Cell Biology U-125 University of Connecticut, Storrs, Connecticut 06269-3125, Department of Horticulture, University of Wisconsin, Madison, Wisconsin 53706

A phosphoinositide-specific phospholipase C activity was identified in oat root (Avena sativa, cv Victory) plasma membranes purified by separation in an aqueous two-phase polymer system. The enzyme is highly active toward inositol phospholipids but only minimally active toward phosphatidylethanolamine and phosphatidylcholine. Activity approaches maximal levels at 200 micromolar phosphatidylinositol 4-phosphate (PIP) and is highly dependent on calcium; it is inhibited by 1 millimolar EGTA and is activated by calcium with an apparent activation constant of 2 micromolar. At 10 micromolar calcium and 200 micromolar inositol phospholipid, the enzyme is specific for phosphatidylinositol 4,5-bisphosphate (PIP2) and PIP, which are hydrolyzed at 10 and 4 times, respectively, the rate of phosphatidylinositol (PI) hydrolysis. The principle water soluble products of hydrolysis, as determined by high performance liquid chromatography, are inositol 1,4,5-trisphosphate from PIP2, inositol 1,4-bisphosphate from PIP, and inositol phosphate from PI.

1 Supported by National Science Foundation grants DMB 86-07857 to R. C. C. and Ruth L. Satter and DCB 8905259 to R. C. C. and by University of Connecticut Research Foundation grant 35-105 to R. C. C.




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Y.-Y. Pan, X. Wang, L.-G. Ma, and D.-Y. Sun
Characterization of Phosphatidylinositol-Specific Phospholipase C (PI-PLC) from Lilium daviddi Pollen
Plant Cell Physiol., October 1, 2005; 46(10): 1657 - 1665.
[Abstract] [Full Text] [PDF]


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