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Molecular and Enzymatic Characterization of Three
Phosphoinositide-Specific Phospholipase C Isoforms from
Potato1
Joachim Kopka,
Christophe Pical,
Julie E. Gray, and
Bernd Müller-Röber*
Max-Planck-Institut für Molekulare Pflanzenphysiologie,
Karl-Liebknecht-Strasse 25, Haus 20, D-14476 Golm/Potsdam, Germany
(J.K., B.M.-R.); and Department of Molecular Biology and
Biotechnology, University of Sheffield, P.O. Box 594, Sheffield,
S10 2UH, United Kingdom (C.P., J.E.G.)
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-tris-phosphate 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 µm
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.
1
The European Molecular Biology Organization and
the Biotechnology and Biological Science Research Council are
acknowledged for their support in providing a short-term fellowship to
C.P. and a research grant to J.E.G.
*
Corresponding author; e-mail mueller{at}mpimp-golm.mpg.de; fax
49-331-977-2301.
Plant Physiol. (1998) 116: 239-250
Copyright Clearance Center: 0032-0889/98/116/0239/12
© 1998 American Society of Plant Physiologists
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