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Polyphosphoinositide phospholipase C and evidence for inositol-phosphate-hydrolysing activities in the plasma-membrane fraction from light-grown wheat (Triticum aestivum L.) leaves

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Abstract

The phospholipase C (PLC; EC 3.1.4.3) activity in isolated plasma membranes of light-grown wheat (Triticum aestivum L. cv. Prelude) leaves was investigated. The activity against the polyphosphoinositides was strongly dependent on Ca2+ and was affected by the anionic detergent deoxycholate (DOC). In the presence of 20 μM Ca2+ the PLC activity preferred phosphatidylinositol 4,5-bisphosphate (PIP2) over phosphatidylinositol 4-monophosphate (PIP) as a substrate. Instead, with 1 mM Ca2+ the enzyme clearly favoured PIP. In addition, the PIP2-PLC activity was increased by Mg2+ and in the presence of GTP, guanosine 5′-(γ-thio)-triphosphate as well as ATP, CTP, guanosine 5′-diphosphate and guanosine 5′-(β-thio)-diphosphate. Further analysis showed that a molybdate-sensitive phosphatase activity catalysing the dephosphorylation of inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) is also associated with the plasma-membrane vesicles. Dephosphorylation of Ins(1,4,5)P3 was reduced in the presence of GTP or by inclusion of the unspecific phosphatase inhibitor molybdate. The results indicate the presence of a PIP2-PLC activity and the presence of a molybdate-sensitive phosphatase activity in wheat plasma-membrane vesicles.

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Abbreviations

DOC:

deoxycholate

IDPase:

inosine 5′-diphosphatase

InsPs :

inositol phosphates, the numbering at the end indicates the number of phosphate residues and when their positions on the inositol ring are known they are indicated in parentheses, i.e.

Ins(1,4,5)P3 :

inositol 1,4,5-trisphosphate

PIP:

phosphatidylinositol 4-monophosphate

PIP2 :

phosphatidylinositol 4,5-bisphosphate

PLC:

phospholipase C

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Authors and Affiliations

  1. Institut für Biologie III, Biochemie der Pflanzen, RWTH Aachen, Worringerweg 1, D-52074, Aachen, Germany

    Michael C. Arz & Hans J. Grambow

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  1. Michael C. Arz
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  2. Hans J. Grambow
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This work was financially supported by grant from the Deutsche Forschungsgemeinschaft (DFG). M. C. Arz gratefully acknowledges the support of a Graduiertenstipendium des Landes Nordrhein-Westfalen (Germany). We wish to thank S. Laden and G.E. Grambow for assistance.

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Arz, M.C., Grambow, H.J. Polyphosphoinositide phospholipase C and evidence for inositol-phosphate-hydrolysing activities in the plasma-membrane fraction from light-grown wheat (Triticum aestivum L.) leaves. Planta 195, 57–62 (1994). https://doi.org/10.1007/BF00206292

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  • DOI: https://doi.org/10.1007/BF00206292

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