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Selective and powerful stress gene expression in Arabidopsis in response to malondialdehyde.

By H. Weber, A. Chételat, P. Reymond and E.E. Farmer

Abstract

The provenance, half-life and biological activity of malondialdehyde (MDA) were investigated in Arabidopsis thaliana. We provide genetic confirmation of the hypothesis that MDA originates from fatty acids containing more than two methylene-linked double bonds, showing that tri-unsaturated fatty acids are the in vivo source of up to 75% of MDA. The abundance of the combined pool of free and reversibly bound MDA did not change dramatically in stress, although a significant increase in the free MDA pool under oxidative conditions was observed. The half-life of infiltrated MDA indicated rapid metabolic turnover/sequestration. Exposure of plants to low levels of MDA using a recently developed protocol powerfully upregulated many genes on a cDNA microarray with a bias towards those implicated in abiotic/environmental stress (e.g. ROF1 and XERO2). Remarkably, and in contrast to the activities of other reactive electrophile species (i.e. small vinyl ketones), none of the pathogenesis-related (PR) genes tested responded to MDA. The use of structural mimics of MDA isomers suggested that the propensity of the molecule to act as a cross-linking/modifying reagent might contribute to the activation of gene expression. Changes in the concentration/localisation of unbound MDA in vivo could strongly affect stress-related transcription

Topics: Arabidopsis/drug effects; Arabidopsis/genetics; Arabidopsis Proteins/genetics; Cross-Linking Reagents/pharmacology; DNA-Binding Proteins/genetics; Drug Stability; Fatty Acids, Unsaturated/metabolism; Gene Expression/drug effects; Genes, Plant/drug effects; Genes, Reporter; Half-Life; Heat-Shock Proteins/genetics; Malondialdehyde/metabolism; Malondialdehyde/pharmacology; Mutation; Oligonucleotide Array Sequence Analysis; Plants, Genetically Modified; Signal Transduction; Tacrolimus Binding Proteins
Publisher: 'Wiley'
Year: 2004
DOI identifier: 10.1111/j.1365-313X.2003.02013.x
OAI identifier: oai:serval.unil.ch:BIB_1DF20CFEDD85
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