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Acylated monogalactosyl diacylglycerol: Prevalence in the plant kingdom and identification of an enzyme catalyzing galactolipid head group acylation in Arabidopsis thaliana

Journal article
Authors Anders K. Nilsson
Oscar Johansson
Per Fahlberg
Murali Kommuri
Mats H. Töpel
Lovisa Bodin
Per Sikora
Masoomeh Modarres
Sophia K Ekengren
Nguyen Chi Tam
Edward E Farmer
Olof Olsson
Mats Ellerström
Mats X. Andersson
Published in The Plant Journal
Volume 84
Issue 6
Pages 1152–1166
ISSN 0960-7412
Publication year 2015
Published at Department of Biological and Environmental Sciences
Pages 1152–1166
Language en
Links dx.doi.org/10.1111/tpj.13072
Keywords Acylated MGDG;Galactolipids;thylakoid membrane; Arabidopsis thaliana ;Wounding;hypersensitive response; Avena sativa
Subject categories Molecular biology, Bioinformatics and Systems Biology

Abstract

The lipid phase of the thylakoid membrane is mainly composed of the galalctolipids mono- and digalactosyl diacylglycerol (MGDG and DGDG, respectively). It has been known since the late sixties that MGDG can be acylated with a third fatty acid to the galactose head group (acyl-MGDG) in plant leaf homogenates. In certain brassicaceous plants like Arabidopsis thaliana, the acyl-MGDG frequently incorporates oxidized fatty acids in the form of the jasmonic acid precursor 12-oxo-phytodienoic acid (OPDA). In the present study we further investigated the distribution of acylated and OPDA-containing galactolipids in the plant kingdom. While acyl-MGDG was found to be ubiquitous in green tissue of plants ranging from non-vascular plants to angiosperms, OPDA-containing galactolipids were only present in plants from a few genera A candidate protein responsible for the acyl transfer was identified in Avena sativa (oat) leaf tissue using biochemical fractionation and proteomcs. Knockout of the orthologous gene in A. thaliana resulted in an almost total elimination of the ability to form both non-oxidized and OPDA-containing acyl-MGDG. In addition, heterologous expression of the A. thaliana gene in E. coli demonstrated that the protein catalyzed acylation of MGDG. We thus demonstrate that a phylogenetically conserved enzyme is responsible for the accumulation of acyl-MGDG in A. thaliana. The activity of this enzyme in vivo is strongly enhanced by freezing damage and the hypersensitive response.

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