JXB Advance Access originally published online on March 19, 2008
Journal of Experimental Botany 2008 59(6):1267-1277; doi:10.1093/jxb/ern037
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© 2008 The Author(s).
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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RESEARCH PAPER |
Immunocytochemical localization of Pisum sativum TRXs f and m in non-photosynthetic tissues
1Departamento de Bioquímica, Biología Celular y Molecular de Plantas, Estación Experimental del Zaidín (CSIC), C/ Prof. Albareda 1, E-18008-Granada, Spain
2Laboratoire Génome et Développement des Plantes, Université de Perpignan, UMR 5096 CNRS-UP-IRD, F-66860 Perpignan, France
3Laboratoire d'Agrophysiologie, EI Purpan, F-31076 Toulouse cedex 3, France
4Instituto de Bioquímica Vegetal y Fotosíntesis, Universidad de Sevilla y CSIC, Avda. Américo Vespucio 49, E-41092-Sevilla, Spain
* Present address and to whom correspondence should be sent: Institut des Sciences du Végétal, UPR2355-CNRS Bt23, Centre National de la Recherche Scientifique, F-91198 Gif/Yvette cedex France. E-mail: jose.traverso{at}isv.cnrs-gif.fr
Plants are the organisms containing the most complex multigenic family for thioredoxins (TRX). Several types of TRXs are targeted to chloroplasts, which have been classified into four subgroups: m, f, x, and y. Among them, TRXs f and m were the first plastidial TRXs characterized, and their function as redox modulators of enzymes involved in carbon assimilation in the chloroplast has been well-established. Both TRXs, f and m, were named according to their ability to reduce plastidial fructose-1,6-bisphosphatase (FBPase) and malate dehydrogenase (MDH), respectively. Evidence is presented here based on the immunocytochemistry of the localization of f and m-type TRXs from Pisum sativum in non-photosynthetic tissues. Both TRXs showed a different spatial pattern. Whilst PsTRXm was localized to vascular tissues of all the organs analysed (leaves, stems, and roots), PsTRXf was localized to more specific cells next to xylem vessels and vascular cambium. Heterologous complementation analysis of the yeast mutant EMY63, deficient in both yeast TRXs, by the pea plastidial TRXs suggests that PsTRXm, but not PsTRXf, is involved in the mechanism of reactive oxygen species (ROS) detoxification. In agreement with this function, the PsTRXm gene was induced in roots of pea plants in response to hydrogen peroxide.
Key words: Heterologous complementation, oxidative stress, pea, Pisum sativum, thioredoxin, vascular tissue, yeast EMY63
Received 20 December 2007; Revised 22 January 2008 Accepted 22 January 2008
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