TY - JOUR
T1 - A defect in glyoxysomal fatty acid β-oxidation reduces jasmonic acid accumulation in Arabidopsis
AU - Afitlhile, M. M.
AU - Fukushige, H.
AU - Nishimura, M.
AU - Hildebrand, D. F.
PY - 2005/6
Y1 - 2005/6
N2 - The final steps of jasmonic acid (JA) biosynthesis are thought to involve peroxisomal β-oxidation, but this has not been directly demonstrated. The last and key step in fatty acid β-oxidation is catalyzed by 3-ketoacyl-CoA thiolase (KAT) (EC 2.3.1.16). A mutant of Arabidopsis thaliana ecotype Landsberg erecta, which lacks a functional KAT protein and is defective in glyoxysomal fatty acid β-oxidation has been reported. In this study, the mutant was found to accumulate reduced level of JA in both its wounded cotyledons and leaves, while only the cotyledons accumulate 3-oxo-2-(pent-2′-enyl)- cyclopentane-1-octanoic acid (OPC-8:0). This indicates that a defect in one of the thiolase isoenzymes impairs β-oxidation of OPC-8:0 to JA. The mutant had sufficient thiolase activity for the synthesis of JA in the unwounded but not in the wounded tissues. Activities of the enzymes in the JA pathway that catalyze the steps, which precede β-oxidation were not altered by the mutation in a thiolase protein. Thus, reduced levels of JA in the wounded tissues of the mutant were attributed to the defect in a thiolase protein.
AB - The final steps of jasmonic acid (JA) biosynthesis are thought to involve peroxisomal β-oxidation, but this has not been directly demonstrated. The last and key step in fatty acid β-oxidation is catalyzed by 3-ketoacyl-CoA thiolase (KAT) (EC 2.3.1.16). A mutant of Arabidopsis thaliana ecotype Landsberg erecta, which lacks a functional KAT protein and is defective in glyoxysomal fatty acid β-oxidation has been reported. In this study, the mutant was found to accumulate reduced level of JA in both its wounded cotyledons and leaves, while only the cotyledons accumulate 3-oxo-2-(pent-2′-enyl)- cyclopentane-1-octanoic acid (OPC-8:0). This indicates that a defect in one of the thiolase isoenzymes impairs β-oxidation of OPC-8:0 to JA. The mutant had sufficient thiolase activity for the synthesis of JA in the unwounded but not in the wounded tissues. Activities of the enzymes in the JA pathway that catalyze the steps, which precede β-oxidation were not altered by the mutation in a thiolase protein. Thus, reduced levels of JA in the wounded tissues of the mutant were attributed to the defect in a thiolase protein.
KW - 12-Oxo-phytodienoic acid
KW - Arabidopsis
KW - Jasmonic acid
KW - OPC-8:0
KW - Thiolase
KW - ped1
KW - β-oxidation
UR - http://www.scopus.com/inward/record.url?scp=22244440848&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=22244440848&partnerID=8YFLogxK
U2 - 10.1016/j.plaphy.2005.03.016
DO - 10.1016/j.plaphy.2005.03.016
M3 - Article
C2 - 15979881
AN - SCOPUS:22244440848
SN - 0981-9428
VL - 43
SP - 603
EP - 609
JO - Plant Physiology and Biochemistry
JF - Plant Physiology and Biochemistry
IS - 6
ER -