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J. Biol. Chem., Vol. 277, Issue 35, 31994-32002, August 30, 2002
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From the A sensitive approach based on electrospray
ionization tandem mass spectrometry has been employed to profile
membrane lipid molecular species in Arabidopsis undergoing
cold and freezing stresses. Freezing at a sublethal temperature induced
a decline in many molecular species of phosphatidylcholine (PC),
phosphatidylethanolamine (PE), and phosphatidylglycerol (PG) but
induced an increase in phosphatidic acid (PA) and lysophospholipids. To
probe the metabolic steps generating these changes, lipids of
Arabidopsis deficient in the most abundant phospholipase D,
PLD
Profiling Membrane Lipids in Plant Stress Responses
ROLE OF PHOSPHOLIPASE D
IN FREEZING-INDUCED LIPID
CHANGES IN ARABIDOPSIS*
§,,
,, and
Division of Biology, Ackert Hall,
Kansas State University, Manhattan, Kansas 66506, the ¶ Department
of Biochemistry, Willard Hall, Kansas State University, Manhattan,
Kansas 66506, the Mass Spectrometry Laboratory, Malott Hall,
University of Kansas, Lawrence, Kansas 66045, and the
** Division of Horticulture, Throckmorton Hall, Kansas State
University, Manhattan, Kansas 66506
, were analyzed. The PC content dropped only half as much, and PA
levels rose only half as high in the PLD-deficient plants as in
wild-type plants. In contrast, neither PE nor PG levels decreased
significantly more in wild-type plants than in PLD-deficient plants.
These data suggest that PC, rather than PE and PG, is the major
in vivo substrate of PLD. The action of PLD during
freezing is of special interest because Arabidopsis plants
that are deficient in PLD have improved tolerance to freezing. The
greater loss of PC and increase in PA in wild-type plants as compared
with PLD-deficient plants may be responsible for destabilizing
membrane bilayer structure, resulting in a greater propensity toward
membrane fusion and cell death in wild-type plants.
*
This work was supported by National Science Foundation Grant
MCB-0110979 (to X. W., R. W., and T. D. W.) and
funds from the Kansas State University Plant Biotechnology Center (to
X. W. and R. W.). This is contribution 02-496-J from the
Kansas Agricultural Experiment Station.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence may be addressed: Dept. of Biochemistry,
Kansas State University, Manhattan, KS 66506. Tel.: 785-532-6422; Fax:
785-532-6653; E-mail: wangs@ksu.edu.
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