Molecular and enzymatic characterization of three phosphoinositide-specific phospholipase C isoforms from potato

Plant Physiology
J KopkaB Müller-Röber

Abstract

Many cellular responses to stimulation of cell-surface receptors by extracellular signals are transmitted across the plasma membrane by hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2), which is cleaved into diacylglycerol and inositol-1,4,5-trisphosphate by phosphoinositide-specific phospholipase C (PI-PLC). We present structural, biochemical, and RNA expression data for three distinct PI-PLC isoforms, StPLC1, StPLC2, and StPLC3, which were cloned from a guard cell-enriched tissue preparation of potato (Solanum tuberosum) leaves. All three enzymes contain the catalytic X and Y domains, as well as C2-like domains also present in all PI-PLCs. Analysis of the reaction products obtained from PIP2 hydrolysis unequivocally identified these enzymes as genuine PI-PLC isoforms. Recombinant StPLCs showed an optimal PIP2-hydrolyzing activity at 10 microM Ca2+ and were inhibited by Al3+ in equimolar amounts. In contrast to PI-PLC activity in plant plasma membranes, however, recombinant enzymes could not be activated by Mg2+. All three stplc genes are expressed in various tissues of potato, including leaves, flowers, tubers, and roots, and are affected by drought stress in a gene-specific manner.

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Citations

Jul 27, 2007·Molecular Biotechnology·Ileana Echevarría-MachadoCésar De Los Santos-Briones
Nov 30, 2011·Plant Molecular Biology·Sunny D Rupwate, Ram Rajasekharan
Sep 13, 2011·Applied Biochemistry and Biotechnology·Manoj Kumar GoelArun Kumar Kukreja
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Jan 18, 2017·Journal of Integrative Plant Biology·Ahmed M Abd-El-Haliem, Matthieu H A J Joosten

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