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Plant Physiol, May 2001, Vol. 126, pp. 267-277
Induction of Lipid Metabolic Enzymes during the Endoplasmic
Reticulum Stress Response in Plants1
Karin J.
Shank,2
Pei
Su,3
Irena
Brglez,
Wendy F.
Boss,
Ralph E.
Dewey,* and
Rebecca S.
Boston
Departments of Crop Science (K.J.S., R.E.D.) and Botany (K.J.S.,
P.S., I.B., W.F.B., R.S.B), Boxes 7620 and 7612, North Carolina State
University, Raleigh, North Carolina 27695
The endoplasmic reticulum (ER) stress response is a signal
transduction pathway activated by the perturbation of normal ER metabolism. We used the maize (Zea mays)
floury-2 (fl2) mutant and soybean
(Glycine max) suspension cultures treated with
tunicamycin (Tm) to investigate the ER stress response as it relates to
phospholipid metabolism in plants. Four key phospholipid biosynthetic
enzymes, including DG kinase and phosphatidylinositol (PI) 4-phosphate 5-kinase were up-regulated in the fl2 mutant,
specifically in protein body fractions where the mutation has its
greatest effect. The third up-regulated enzyme, choline-phosphate
cytidylyltransferase, was regulated by fl2 gene dosage
and developmental signals. Elevated accumulation of the fourth enzyme,
PI 4-kinase, was observed in the fl2 endosperm and
soybean cells treated with Tm. The activation of these phospholipid
biosynthetic enzymes was accompanied by alterations in membrane lipid
synthesis and accumulation. The fl2 mutant exhibited
increased PI content in protein body membranes at 18 d after
pollination and more than 3-fold higher triacylglycerol accumulation in
the endosperm by 36 d after pollination. Incorporation of
radiolabeled acetate into phospholipids in soybean culture cells
increased by about 30% with Tm treatment. The coordinated regulation
of ER stress related proteins and multiple components of phospholipid
biosynthesis is consistent with signaling through a common pathway. We
postulate that the plant ER stress response has an important role in
general plant metabolism, and more specifically in integrating the
synthesis of protein and lipid reserves to allow proper seed formation.
1
This work was supported by the U.S. Department
of Energy (grant no. DE-FG02-00ER150065 to R.S.B., R.E.D., and
W.F.B.), by the National Science Foundation (grant nos. MCB96-04285
[to W.F.B.], IBN-9513582 [to R.E.D.], and MCB93-17303 [to
R.S.B.]), by the North Carolina Agricultural Research Service (to
W.F.B., R.S.B., and R.E.D.), and by the National Science Foundation for
Interdisciplinary Research Training Group on Transgenic Plant
Technology for Laboratory and Field Applications (fellowship no.
BIR-9420689 to K.J.S.).
2
Present address: BASF Plant Sciences, Research Triangle
Park, NC 27709.
3
Present address: Department of Biochemistry, Box 7622, North Carolina State University, Raleigh, NC 27695.
*
Corresponding author; email ralph_dewey{at}ncsu.edu; fax
919-515-7959.
© 2001 American Society of Plant Physiologists
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