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The activity of HYDROPEROXIDE LYASE 1 regulates accumulation of galactolipids containing 12-oxo-phytodienoic acid in Arabidopsis

Journal article
Authors Anders K. Nilsson
Per Fahlberg
Oskar N. Johansson
M. Hamberg
Mats X. Andersson
Mats Ellerström
Published in Journal of Experimental Botany
Volume 67
Issue 17
Pages 5133-5144
ISSN 0022-0957
Publication year 2016
Published at Department of Biological and Environmental Sciences
Pages 5133-5144
Language en
Links dx.doi.org/10.1093/jxb/erw278
Keywords Acyl-MGDG, arabidopsides, Arabidopsis accessions, hydroperoxide lyase, jasmonates, OPDA, natural variation, allene oxide cyclase, green leaf volatiles, jasmonic acid, hypersensitive response, plant-defense, experimental populations, genetic architecture, signal-transduction, stress-response, complex, traits, Plant Sciences
Subject categories Biological Sciences

Abstract

Arabidopsis produces galactolipids containing esters of 12-oxo-phytodienoic acid (OPDA) and dinor-12-oxo-phytodienoic acid (dnOPDA). These lipids are referred to as arabidopsides and accumulate in response to abiotic and biotic stress. We explored the natural genetic variation found in 14 different Arabidopsis accessions to identify genes involved in the formation of arabidopsides. The accession C24 was identified as a poor accumulator of arabidopsides whereas the commonly used accession Col-0 was found to accumulate comparably large amounts of arabidopsides in response to tissue damage. A quantitative trait loci analysis of an F-2 population created from a cross between C24 and Col-0 located a region on chromosome four strongly linked to the capacity to form arabidopsides. Expression analysis of HYDROPEROXIDE LYASE 1 (HPL1) showed large differences in transcript abundance between accessions. Transformation of Col-0 plants with the C24 HPL1 allele under transcriptional regulation of the 35S promoter revealed a strong negative correlation between HPL1 expression and arabidopside accumulation after tissue damage, thereby strengthening the view that HPL1 competes with ALLENE OXIDE SYNTHASE (AOS) for lipid-bound hydroperoxide fatty acids. We further show that the last step in the synthesis of galactolipid-bound OPDA and dnOPDA from unstable allene oxides is exclusively enzyme-catalyzed and not the result of spontaneous cyclization. Thus, the results presented here together with previous studies suggest that all steps in arabidopside biosynthesis are enzyme-dependent and apparently all reactions can take place with substrates being esterified to galactolipids.

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