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,
from Arabidopsis
(Received for publication, November 15, 1996, and in revised form, January 2, 1997)
From the Department of Biochemistry, Kansas State University,
Manhattan, Kansas 66506
A novel plant phospholipase D (PLD; EC 3.1.4.4)
activity, which is dependent on phosphatidylinositol 4,5-bisphosphate
(PIP2) and nanomolar concentrations of calcium, has been
identified in Arabidopsis. This report describes the
cloning, expression, and characterization of an Arabidopsis
cDNA that encodes this PLD. We have designated names of PLD
for
this PIP2-dependent PLD and PLD
for the
previously characterized PIP2-independent PLD that requires
millimolar Ca2+ for optimal activity. The PLD cDNA
contains an open reading frame of 2904 nucleotides coding for a
968-amino acid protein of 108,575 daltons. Expression of this PLD
cDNA clone in Escherichia coli results in the
accumulation of a functional PLD having PLD, but not PLD,
activity. The activity of the expressed PLD is dependent on
PIP2 and submicromolar amounts of Ca2+,
inhibited by neomycin, and stimulated by a soluble factor from plant
extracts. Sequence analysis reveals that PLD is evolutionarily divergent from PLD and that its N terminus contains a regulatory Ca2+-dependent phospholipid-binding (C2) domain
that is found in a number of signal transducing and membrane
trafficking proteins.
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