title: Physiological relevance of plant 2-Cys peroxiredoxin overoxidation level and oligomerization status.
abstract: Peroxiredoxins are ubiquitous thioredoxin-dependent peroxidases presumed to display, upon environmental constraints, a chaperone function resulting from a redox-dependent conformational switch. In this work, using biochemical and genetic approaches, we aimed to unravel the factors regulating the redox status and the conformation of the plastidial 2-Cys peroxiredoxin (2-Cys PRX) in plants. In Arabidopsis, we show that in optimal growth conditions, the overoxidation level mainly depends on the availability of thioredoxin-related electron donors, but not on sulfiredoxin, the enzyme reducing the 2-Cys PRX overoxidized form. We also observed that upon various physiological temperature, osmotic and light stress conditions, the overoxidation level and oligomerization status of 2-Cys PRX can moderately vary depending on the constraint type. Further, no major change was noticed regarding protein conformation in water-stressed Arabidopsis, barley and potato plants, whereas species-dependent up- and down-variations in overoxidation were observed. In contrast, both 2-Cys PRX overoxidation and oligomerization were strongly induced during a severe oxidative stress generated by methyl viologen. From these data, revealing that the oligomerization status of plant 2-Cys PRX does not exhibit important variation and is not tightly linked to the protein redox status upon physiologically relevant environmental constraints, the possible in planta functions of 2-Cys PRX are discussed.
authors.affiliation: CEA, DSV, IBEB, Laboratoire d'Ecophysiologie Moléculaire des Plantes, Saint-Paul-lez-Durance, F-13108, France.|CNRS, UMR 7265, Biologie Végétale and Microbiologie Environnementale, Saint-Paul-lez-Durance, F-13108, France.|Aix-Marseille Université, Saint-Paul-lez-Durance, F-13108, France.
authors.forename: Delphine
authors.initials: D
authors.lastname: Cerveau
authors.affiliation: CEA, DSV, IBEB, Laboratoire d'Ecophysiologie Moléculaire des Plantes, Saint-Paul-lez-Durance, F-13108, France.|CNRS, UMR 7265, Biologie Végétale and Microbiologie Environnementale, Saint-Paul-lez-Durance, F-13108, France.|Aix-Marseille Université, Saint-Paul-lez-Durance, F-13108, France.
authors.forename: Djelloul
authors.initials: D
authors.lastname: Ouahrani
authors.affiliation: CEA, DSV, IBEB, Laboratoire d'Ecophysiologie Moléculaire des Plantes, Saint-Paul-lez-Durance, F-13108, France.|CNRS, UMR 7265, Biologie Végétale and Microbiologie Environnementale, Saint-Paul-lez-Durance, F-13108, France.|Aix-Marseille Université, Saint-Paul-lez-Durance, F-13108, France.|Université de Khemis Miliana, Faculté des Sciences de la Nature et de la Vie et des Sciences de la Terre, Ain Defla, Khemis Miliana, 44225, Algérie.
authors.forename: Mohamed Amine
authors.initials: MA
authors.lastname: Marok
authors.affiliation: CNRS, UMR 7265, Biologie Végétale and Microbiologie Environnementale, Saint-Paul-lez-Durance, F-13108, France.|Aix-Marseille Université, Saint-Paul-lez-Durance, F-13108, France.|CEA, DSV, IBEB, Laboratoire de Bioénergétique Cellulaire, Saint-Paul-lez-Durance, F-13108, France.
authors.forename: Laurence
authors.initials: L
authors.lastname: Blanchard
authors.affiliation: CEA, DSV, IBEB, Laboratoire d'Ecophysiologie Moléculaire des Plantes, Saint-Paul-lez-Durance, F-13108, France.|CNRS, UMR 7265, Biologie Végétale and Microbiologie Environnementale, Saint-Paul-lez-Durance, F-13108, France.|Aix-Marseille Université, Saint-Paul-lez-Durance, F-13108, France.
authors.forename: Pascal
authors.initials: P
authors.lastname: Rey
mesh_terms: D017360:Arabidopsis / Q000201:enzymology* / Q000235:genetics / Q000502:physiology; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism*; D003545:Cysteine / Q000378:metabolism; D035264:Flowers / Q000201:enzymology / Q000235:genetics / Q000502:physiology; D005638:Fruit / Q000201:enzymology / Q000235:genetics / Q000502:physiology; D001467:Hordeum / Q000201:enzymology* / Q000235:genetics / Q000502:physiology; D008027:Light; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D050862:Oxidoreductases Acting on Sulfur Group Donors / Q000378:metabolism; D054464:Peroxiredoxins / Q000235:genetics / Q000378:metabolism*; D018515:Plant Leaves / Q000201:enzymology / Q000235:genetics / Q000502:physiology; D018517:Plant Roots / Q000201:enzymology / Q000235:genetics / Q000502:physiology; D018547:Plant Stems / Q000201:enzymology / Q000235:genetics / Q000502:physiology; D058105:Polymerization; D011487:Protein Conformation; D021381:Protein Transport; D011994:Recombinant Proteins; D011198:Solanum tuberosum / Q000201:enzymology* / Q000235:genetics / Q000502:physiology; D013045:Species Specificity; D013879:Thioredoxins / Q000378:metabolism
chemical_list: D029681:Arabidopsis Proteins; D011994:Recombinant Proteins; D013879:Thioredoxins; C493631:2-Cys peroxiredoxin A, Arabidopsis; D054464:Peroxiredoxins; D050862:Oxidoreductases Acting on Sulfur Group Donors; C520419:sulfiredoxin protein, Arabidopsis; D003545:Cysteine
keywords: 2-Cys peroxiredoxin; environmental constraints; higher plants; oligomerization; overoxidation; plastid