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Plant Physiol, June 2000, Vol. 123, pp. 711-724
Cytochrome P450-Dependent Metabolism of Oxylipins in Tomato.
Cloning and Expression of Allene Oxide Synthase and Fatty Acid
Hydroperoxide Lyase1
Gregg A.
Howe,*
Gyu In
Lee,
Aya
Itoh,
Lei
Li, and
Amy E.
DeRocher2
Department of Energy-Plant Research Laboratory (G.A.H., G.I.L.,
A.I., L.L., A.E.D.) and Department of Biochemistry (G.A.H.), Michigan
State University, East Lansing, Michigan 48824
Allene oxide synthase (AOS) and fatty acid hydroperoxide lyase
(HPL) are plant-specific cytochrome P450s that commit fatty acid
hydroperoxides to different branches of oxylipin metabolism. Here we
report the cloning and characterization of AOS (LeAOS) and HPL (LeHPL) cDNAs from tomato (Lycopersicon
esculentum). Functional expression of the cDNAs in
Escherichia coli showed that LeAOS and
LeHPL encode enzymes that metabolize 13- but not
9-hydroperoxide derivatives of C18 fatty acids. LeAOS was
active against both 13S-hydroperoxy-9(Z),11(E),15(Z)-octadecatrienoic
acid (13-HPOT) and
13S-hydroperoxy-9(Z),11(E)-octadecadienoic
acid, whereas LeHPL showed a strong preference for 13-HPOT. These
results suggest a role for LeAOS and
LeHPL in the metabolism of 13-HPOT to jasmonic acid and
hexenal/traumatin, respectively. LeAOS expression was detected in all organs of the plant. In contrast, LeHPL
expression was predominant in leaves and flowers. Damage inflicted to
leaves by chewing insect larvae led to an increase in the local and
systemic expression of both genes, with LeAOS showing
the strongest induction. Wound-induced expression of
LeAOS also occurred in the def-1 mutant that is deficient in octadecanoid-based signaling of defensive proteinase inhibitor genes. These results demonstrate that tomato uses
genetically distinct signaling pathways for the regulation of different
classes of wound responsive genes.
1
This work was supported by the U.S. Department
of Agriculture/National Research Initiative Program (grant no. 9801335)
and by an All University Research Initiation Grant from Michigan State University.
2
Present address: Seattle Biomedical Research
Institute, 4 Nickerson Street, Suite 200, Bothell, WA 98021.
*
Corresponding author; e-mail howeg{at}msu.edu; fax 517-353-9168.
© 2000 American Society of Plant Physiologists
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