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Plant Physiol, October 2000, Vol. 124, pp. 693-702
Abscisic Acid Stimulation of Phospholipase D in the Barley
Aleurone Is G-Protein-Mediated and Localized to the Plasma
Membrane1
Sian
Ritchie and
Simon
Gilroy*
Department of Biology, Pennsylvania State University, 208 Mueller
Laboratory, University Park, Pennsylvania 16802
We have previously determined that phospholipase D (PLD) is
activated by abscisic acid (ABA), and this activation is required for
the ABA response of the cereal aleurone cell. In this study, ABA-stimulated PLD activity was reconstituted in vitro in microsomal membranes prepared from aleurone protoplasts. The transient nature (20 min) and degree (1.5- to 2-fold) of activation in vitro were similar to
that measured in vivo. Stimulation by ABA was only apparent in the
membrane fraction and was associated with a fraction enriched in plasma
membrane. These results suggest that an ABA receptor system and
elements linking it to PLD activation are associated with the aleurone
plasma membrane. The activation of PLD in vitro by ABA was dependent on
the presence of GTP. Addition of GTP S transiently stimulated
PLD in an ABA-independent manner, whereas treatment with GDP S
or pertussis toxin blocked the PLD activation by ABA. Application of
pertussis toxin to intact aleurone protoplasts inhibited the ability of
ABA to activate PLD as well as antagonizing the ability of ABA to
down-regulate gibberellic acid-stimulated  -amylase production. All
of these data support the hypothesis that ABA stimulation of PLD
activity occurs at the plasma membrane and is mediated by G-protein activity.
1
This work was supported by a grant from the U.S.
Department of Agriculture (to S.G.).
*
Corresponding author; e-mail sxg12{at}psu.edu; fax
814-865-9131.
© 2000 American Society of Plant Physiologists
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