title: Plant glutathione peroxidases are functional peroxiredoxins distributed in several subcellular compartments and regulated during biotic and abiotic stresses.
abstract: We provide here an exhaustive overview of the glutathione (GSH) peroxidase (Gpx) family of poplar (Populus trichocarpa). Although these proteins were initially defined as GSH dependent, in fact they use only reduced thioredoxin (Trx) for their regeneration and do not react with GSH or glutaredoxin, constituting a fifth class of peroxiredoxins. The two chloroplastic Gpxs display a marked selectivity toward their electron donors, being exclusively specific for Trxs 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 (cysteine [Cys]-107 and Cys-155) of the three conserved Cys, 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 sodium dodecyl sulfate-polyacrylamide gel electrophoresis 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 colocalizing in mitochondria, suggesting a broad distribution of Gpxs in plant cells. The abundance of some 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 to both biotic and abiotic stress conditions.
authors.affiliation: Unité Mixte de Recherche Institut National de la Recherche Agronomique-Université Henri Poincaré 1136, Université Henri Poincaré, 54506 Vandoeuvre cedex, France.
authors.forename: Nicolas
authors.initials: N
authors.lastname: Navrot
authors.forename: Valérie
authors.initials: V
authors.lastname: Collin
authors.forename: José
authors.initials: J
authors.lastname: Gualberto
authors.forename: Eric
authors.initials: E
authors.lastname: Gelhaye
authors.forename: Masakazu
authors.initials: M
authors.lastname: Hirasawa
authors.forename: Pascal
authors.initials: P
authors.lastname: Rey
authors.forename: David B
authors.initials: DB
authors.lastname: Knaff
authors.forename: Emmanuelle
authors.initials: E
authors.lastname: Issakidis
authors.forename: Jean-Pierre
authors.initials: JP
authors.lastname: Jacquot
authors.forename: Nicolas
authors.initials: N
authors.lastname: Rouhier
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D018506:Gene Expression Regulation, Plant; D018745:Genome, Plant; D005979:Glutathione Peroxidase / Q000032:analysis / Q000737:chemistry / Q000502:physiology*; D049452:Green Fluorescent Proteins / Q000032:analysis; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D010545:Peroxides / Q000378:metabolism; D010802:Phylogeny; D010940:Plant Proteins / Q000032:analysis / Q000737:chemistry / Q000502:physiology*; D032107:Populus / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics; D020033:Protein Isoforms / Q000032:analysis / Q000737:chemistry / Q000502:physiology; D011993:Recombinant Fusion Proteins / Q000032:analysis; D016415:Sequence Alignment; D013379:Substrate Specificity; D013879:Thioredoxins / Q000378:metabolism
chemical_list: D010545:Peroxides; D010940:Plant Proteins; D020033:Protein Isoforms; D011993:Recombinant Fusion Proteins; D049452:Green Fluorescent Proteins; D013879:Thioredoxins; D005979:Glutathione Peroxidase