Ellinger, Dorothea;
Stingl, Nadja;
Kubigsteltig, Ines Ingeborg;
Bals, Thomas;
Juenger, Melanie;
Pollmann, Stephan;
Berger, Susanne;
Schuenemann, Danja;
Mueller, Martin Johannes
DONGLE and DEFECTIVE IN ANTHER DEHISCENCE1 Lipases Are Not Essential for Wound- and Pathogen-Induced Jasmonate Biosynthesis: Redundant Lipases Contribute to Jasmonate Formation
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Medientyp:
E-Artikel
Titel:
DONGLE and DEFECTIVE IN ANTHER DEHISCENCE1 Lipases Are Not Essential for Wound- and Pathogen-Induced Jasmonate Biosynthesis: Redundant Lipases Contribute to Jasmonate Formation
Beschreibung:
<p>Lipases are involved in the generation of jasmonates, which regulate responses to biotic and abiotic stresses. Two sn-1-specific acyl hydrolases, DEFECTIVE IN ANTHER DEHISCENCE1 (DAD1) and DONGLE (DGL), have been reported to be localized in plastids and to be essential and sufficient for jasmonate biosynthesis in Arabidopsis (Arabidopsis thaliana) leaves. Here, we show that levels of 12-oxo-phytodienoic acid (OPDA) and jasmonic acid in three different DGL RNA interference lines and the dad1 mutant were similar to wild-type levels during the early wound response as well as after Pseudomonas infection. Due to the lack of sn-2 substrate specificity, synthesis of dinor OPDA was not expected and also not found to be affected in DGL knockdown and DGL-overexpressing lines. As reported, DAD1 participates in jasmonate formation only in the late wound response. In addition, DGL protein was found to be localized in lipid bodies and not in plastids. Furthermore, jasmonate levels in 16 additional mutants defective in the expression of lipases with predicted chloroplast localization did not show strong differences from wild-type levels after wounding, except for a phospholipase A (PLA) PLA-Iγ1 (At1g06800) mutant line that displayed diminished wound-induced dinor OPDA, OPDA, and jasmonic acid levels. A quadruple mutant defective in four DAD1-like lipases displayed similar jasmonate levels as the mutant line of PLA-Iγ1 after wounding. Hence, we identify PLA-Iγ1 as a novel target gene to manipulate jasmonate biosynthesis. Our results suggest that, in addition to DAD1 and PLA-Iγ1, still unidentified enzymes with sn-1 and sn-2 hydrolase activity are involved in wound- and pathogen-induced jasmonate formation, indicating functional redundancy within the lipase family.</p>