Arabidopsis Chloroplastic Glutathione Peroxidases Play a Role in Cross Talk between Photooxidative Stress and Immune Responses

Christine C.C Chang,Barbara KarpińSka,LucíA Jordá,Michael Melzer,Jane E Parker,Alexey Sotnikov,Stanisław KarpińSki,Ireneusz ŚLesak,Zbigniew Miszalski,Philip M Mullineaux

doi:10.1104/pp.109.135566

Abstract

Glutathione peroxidases (GPXs; EC 1.11.1.9) are key enzymes of the antioxidant network in plants and animals. In order to investigate the role of antioxidant systems in plant chloroplasts, we generated Arabidopsis (Arabidopsis thaliana) transgenic lines that are depleted specifically in chloroplastic (cp) forms of GPX1 and GPX7. We show that reduced cpGPX expression, either in transgenic lines with lower total cpGPX expression (GPX1 and GPX7) or in a gpx7 insertion mutant, leads to compromised photooxidative stress tolerance but increased basal resistance to virulent bacteria. Depletion of both GPX1 and GPX7 expression also caused alterations in leaf cell and chloroplast morphology. Leaf tissues were characterized by shorter and more rounded palisade cells, irregular spongy mesophyll cells, and larger intercellular air spaces compared with the wild type. Chloroplasts had larger and more abundant starch grains than in wild-type and gpx7 mutant plants. Constitutively reduced cpGPX expression also led to higher foliar ascorbic acid, glutathione, and salicylic acid levels in plants exposed to higher light intensities. Our results suggest partially overlapping functions of GPX1 and GPX7. The data further point to specific changes in the chloroplast ascorbate-glutathione cycle due to reduced cpGPX expression, initiating reactive oxygen species and salicylic acid pathways that affect leaf development, light acclimation, basal defense, and cell death programs. Thus, cpGPXs regulate cellular photooxidative tolerance and immune responses.

Highlights

Glutathione peroxidases (GPXs; EC 1.11.1.9) are key enzymes of the antioxidant network in plants and animals
The total GPX activity measured using two substrates, H2O2 and t-butyl hydroperoxide, in the crude foliar extract was not diminished in AS-cpGPX lines 71-90, 71-92, and 71-93 or in the gpx7 null mutant when compared with wild-type plants (Fig. 1B)
GPX activity in isolated intact chloroplasts was reduced in the AS lines and the gpx7 mutant, with AScpGPX 71-93 exhibiting the strongest reduction of wild-type chloroplast activity (Fig. 1C)

Summary

Introduction

Glutathione peroxidases (GPXs; EC 1.11.1.9) are key enzymes of the antioxidant network in plants and animals. We show that reduced cpGPX expression, either in transgenic lines with lower total cpGPX expression (GPX1 and GPX7) or in a gpx insertion mutant, leads to compromised photooxidative stress tolerance but increased basal resistance to virulent bacteria. Depletion of both GPX1 and GPX7 expression caused alterations in leaf cell and chloroplast morphology. The data further point to specific changes in the chloroplast ascorbate-glutathione cycle due to reduced cpGPX expression, initiating reactive oxygen species and salicylic acid pathways that affect leaf development, light acclimation, basal defense, and cell death programs. Plant cells have evolved effective mechanisms to modulate steady-state levels of ROS inside and to some extent outside cells (Mittler, 2002)

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