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ENVIRONMENTAL STRESS AND ADAPTATION TO STRESS

PsTRXh1 and PsTRXh2 Are Both Pea h-Type Thioredoxins with Antagonistic Behavior in Redox Imbalances^1,2

Departamento de Bioquímica, Biología Celular y Molecular de Plantas, Estación Experimental del Zaidín, 18008 Granada, Spain (J.A.T., A.P., M.S., A.C.); Laboratoire Génome et Développement des Plantes, Université de Perpignan, Unité Mixte de Recherche 5096, Centre National de la Recherche Scientifique, 66860 Perpignan, France (F.V., Y.M.); Laboratoire d'Agrophysiologie, Unité Mixte de Recherche 1054 Institut National de la Recherche Agronomique, Ecole Supérieure d'Agriculture de Purpan, 31076 Toulouse cedex 3, France (R.C.); and Instituto de Bioquímica Vegetal y Fotosíntesis, Centro de Investigaciones Científicas Isla de la Cartuja, 41092 Seville, Spain (F.J.C.)

Thioredoxins (TRXs) are small ubiquitous oxidoreductases involved in disulfide bond reduction of a large panel of target proteins. The most complex cluster in the family of plant TRXs is formed by h-type TRXs. In Arabidopsis (Arabidopsis thaliana), nine members of this subgroup were described, which are less well known than their plastidial counterparts. The functional study of type-h TRXs is difficult because of the high number of isoforms and their similar biochemical characteristics, thus raising the question whether they have specific or redundant functions. Type-h TRXs are involved in seed germination and self incompatibility in pollen-pistil interaction. Their function as antioxidants has recently been proposed, but further work is needed to clarify this function in plants. In this study, we describe two new h-type TRXs from pea (Pisum sativum; stated PsTRXh1 and PsTRXh2). By functional complementation of a yeast (Saccharomyces cerevisiae) trx1 trx2 double mutant, we demonstrate that PsTRXh1 is involved in the redox-imbalance control, possibly through its interaction with peroxiredoxins. In contrast, PsTRXh2 provokes a phenotype of hypersensitivity to hydrogen peroxide in the yeast mutant. Furthermore, we show differential gene expression and protein accumulation of the two isoforms, PsTRXh1 protein being abundantly detected in vascular tissue and flowers, whereas PsTRXh2 gene expression was hardly detectable. By comparison with previous data of additional PsTRXh isoforms, our results indicate specific functions for the pea h-type TRXs so far described.

² This paper is dedicated to the loved and esteemed memory of Professor Julio López Gorgé, who died on June 7, 2004, at the age of 69.

³ Present address: Institut des Sciences du Végétal, UPR2355-CNRS Bt23, Centre National de la Recherche Scientifique, F–91198 Gif/Yvette cedex, France.

The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: José A. Traverso (jose.traverso{at}isv.cnrs-gif.fr).

www.plantphysiol.org/cgi/doi/10.1104/pp.106.089524

^* Corresponding author; e-mail jose.traverso{at}isv.cnrs-gif.fr; fax 33–1–69–82–36–07.

Received September 6, 2006; accepted November 6, 2006; published November 10, 2006.

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