Plant Physiology Preview
Published on October 27, 2006; 10.1104/pp.106.089458
Received September 4, 2006
Accepted October 11, 2006
Plant Glutathione Peroxidases Are Functional Peroxiredoxins Distributed in Several Subcellular Compartments and Regulated during Biotic and Abiotic Stresses
Nicolas Navrot , Valérie Collin , José Gualberto , Eric Gelhaye , Masakazu Hirasawa , Pascal Rey , David B. Knaff , Emmanuelle Issakidis , Jean-Pierre Jacquot , and Nicolas Rouhier *
Unité Mixte de Recherche INRA-UHP 1136, Interactions Arbres/Micro-organismes, IFR 110 GEEF, Université Henri Poincaré, Faculté des Sciences, BP 239 54506 Vandoeuvre Cedex, France
CEA/Cadarache, DSV, DEVM, Laboratoire d'Ecophysiologie Moléculaire des Plantes, 13108 Saint-Paul-lez-Durance Cedex, France
Institut de Biologie Moléculaire des Plantes, CNRS 67084 Strasbourg Cedex
Department of Chemistry and Biochemistry, and Center for Biotechnology and Genomics, Texas Tech University, Lubbock, Texas 79409-1061, USA
Institut de Biotechnologie des Plantes, UMR 8618, Université de Paris Sud 91405 Orsay Cedex, France
* Corresponding author; email: nrouhier{at}scbiol.uhp-nancy.fr.
We provide here an exhaustive overview of the glutathione peroxidase (Gpx) family of Populus trichocarpa. Although these proteins were initially defined as glutathione dependent, in fact they use only reduced thioredoxin (Trx) for their regeneration and do not react with glutathione or glutaredoxin, constituting a fifth class of peroxiredoxins. The two chloroplastic Gpxs display a marked selectivity toward their electron donors, being exclusively specific for thioredoxins of the y type for their reduction. In contrast, poplar Gpxs are much less specific with regard to their electron-accepting substrates, reducing hydrogen peroxide and more complex hydroperoxides equally well. Site-directed mutagenesis indicates that the catalytic mechanism and the Trx-mediated recycling process involve only two (Cys 107 and Cys 155) of the three conserved cysteines, which form a disulfide bridge with an oxidation-redox midpoint potential of -295 mV. The reduction/formation of this disulfide is detected both by a shift on SDS PAGE or by measuring the intrinsic tryptophan fluorescence of the protein. The six genes identified coding for Gpxs are expressed in various poplar organs and two of them are localized in the chloroplast, with one co-localizing in mitochondria, suggesting a broad distribution of Gpxs in plant cells. The abundance of some of Gpxs is modified in plants subjected to environmental constraints, generally increasing during fungal infection, water deficit and metal stress, and decreasing during photooxidative stress, showing that Gpx proteins are involved in the response of both biotic and abiotic stress conditions.
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