Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Published on November 10, 2006; 10.1104/pp.106.089524


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Received September 6, 2006
Accepted November 6, 2006

PsTRXh1 and PsTRXh2, are both Pea (Pisum sativum) h-type Thioredoxins with Antagonistic Behaviour in Redox Imbalances

José A. Traverso *, Florence Vignols , Roland Cazalis , Amada Pulido , Mariam Sahrawy , Francisco Javier Cejudo , Yves Meyer , and Ana Chueca

Departamento de Bioquímica, Biología Celular y Molecular de Plantas, Estación Experimental del Zaidín (CSIC), C/ Prof. Albareda 1, 18008-Granada, Spain
Laboratoire Génome et Développement des Plantes, Université de Perpignan, UMR 5096 CNRS-UP-IRD, 66860 Perpignan, France
Laboratoire d'Agrophysiologie, UMR 1054 INRA, ESA Purpan, 31076 Toulouse Cedex 3, France
Instituto de Bioquímica Vegetal y Fotosíntesis, Centro de Investigaciones Científicas Isla de la Cartuja, Avda. Américo Vespucio 49, 41092-Sevilla, Spain

* Corresponding author; email: jose.traverso{at}isv.cnrs-gif.fr.

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 thioredoxins is formed by h-type TRXs. In Arabidopsis thaliana, nine members of this subgroup were described, which are less well known than their plastidial counterparts. The functional study of TRXhs is difficult because of the high number of isoforms and their similar biochemical characteristics, thus arising 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 Pisum sativum (stated PsTRXh1 and PsTRXh2). By functional complementation of a yeast trx1{Delta} trx2{Delta} 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 thioredoxins so far described.




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J Exp BotHome page
J. A. Traverso, F. Vignols, R. Cazalis, A. J. Serrato, P. Pulido, M. Sahrawy, Y. Meyer, F. J. Cejudo, and A. Chueca
Immunocytochemical localization of Pisum sativum TRXs f and m in non-photosynthetic tissues
J. Exp. Bot., April 1, 2008; 59(6): 1267 - 1277.
[Abstract] [Full Text] [PDF]


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J. de Dios Barajas-Lopez, A. J. Serrato, A. Olmedilla, A. Chueca, and M. Sahrawy
Localization in Roots and Flowers of Pea Chloroplastic Thioredoxin f and Thioredoxin m Proteins Reveals New Roles in Nonphotosynthetic Organs
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[Abstract] [Full Text] [PDF]




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