title: The chloroplast membrane associated ceQORH putative quinone oxidoreductase reduces long-chain, stress-related oxidized lipids.
abstract: Under oxidative stress conditions the lipid constituents of cells can undergo oxidation whose frequent consequence is the production of highly reactive α,β-unsaturated carbonyls. These molecules are toxic because they can add to biomolecules (such as proteins and nucleic acids) and several enzyme activities cooperate to eliminate these reactive electrophile species. CeQORH (chloroplast envelope Quinone Oxidoreductase Homolog, At4g13010) is associated with the inner membrane of the chloroplast envelope and imported into the organelle by an alternative import pathway. In the present study, we show that the recombinant ceQORH exhibits the activity of a NADPH-dependent α,β-unsaturated oxoene reductase reducing the double bond of medium-chain (C⩾9) to long-chain (18 carbon atoms) reactive electrophile species deriving from poly-unsaturated fatty acid peroxides. The best substrates of ceQORH are 13-lipoxygenase-derived γ-ketols. γ-Ketols are spontaneously produced in the chloroplast from the unstable allene oxide formed in the biochemical pathway leading to 12-oxo-phytodienoic acid, a precursor of the defense hormone jasmonate. In chloroplasts, ceQORH could detoxify 13-lipoxygenase-derived γ-ketols at their production sites in the membranes. This finding opens new routes toward the understanding of γ-ketols role and detoxification.
authors.affiliation: Univ. Grenoble Alpes, F-38054 Grenoble, France; Commissariat à l'Energie Atomique et aux Energies Alternatives, Direction des Sciences du Vivant, Institut de Recherches en Technologies et Sciences pour le Vivant, F-38054 Grenoble, France; INRA, USC1359, 17 rue des Martyrs, F-38054 Grenoble, France; CNRS, Laboratoire de Physiologie Cellulaire & Végétale, UMR 5168, 17 rue des Martyrs, F-38054 Grenoble, France. Electronic address: gilles.curien@cea.fr.
authors.forename: Gilles
authors.initials: G
authors.lastname: Curien
authors.affiliation: Univ. Grenoble Alpes, F-38054 Grenoble, France; Commissariat à l'Energie Atomique et aux Energies Alternatives, Direction des Sciences du Vivant, Institut de Recherches en Technologies et Sciences pour le Vivant, F-38054 Grenoble, France; INRA, USC1359, 17 rue des Martyrs, F-38054 Grenoble, France; CNRS, Laboratoire de Physiologie Cellulaire & Végétale, UMR 5168, 17 rue des Martyrs, F-38054 Grenoble, France.
authors.forename: Cécile
authors.initials: C
authors.lastname: Giustini
authors.affiliation: Commissariat à l'Energie Atomique et aux Energies Alternatives, Centre de Cadarache, Direction des Sciences du Vivant (DSV), Institut de Biologie Environnementale et Biotechnologie (IBEB), Service de Biologie Végétale et de Microbiologie Environnementale (SBVME), Laboratoire d'Ecophysiologie Moléculaire des Plantes, UMR 7265, Centre National de la Recherche Scientifique (CNRS)/CEA/Aix-Marseille Université, F-13108 Saint-Paul-lez-Durance, France.
authors.forename: Jean-Luc
authors.initials: JL
authors.lastname: Montillet
authors.affiliation: Institut de Biologie Structurale, Univ. Grenoble Alpes, CNRS, CEA, 71 Avenue des Martyrs, 38044 Grenoble, France.
authors.forename: Sarah
authors.initials: S
authors.lastname: Mas-Y-Mas
authors.affiliation: Institut de Biologie Structurale, Univ. Grenoble Alpes, CNRS, CEA, 71 Avenue des Martyrs, 38044 Grenoble, France.
authors.forename: David
authors.initials: D
authors.lastname: Cobessi
authors.affiliation: Institut de Biologie Structurale, Univ. Grenoble Alpes, CNRS, CEA, 71 Avenue des Martyrs, 38044 Grenoble, France.
authors.forename: Jean-Luc
authors.initials: JL
authors.lastname: Ferrer
authors.affiliation: Univ. Grenoble Alpes, F-38054 Grenoble, France; Commissariat à l'Energie Atomique et aux Energies Alternatives, Direction des Sciences du Vivant, Institut de Recherches en Technologies et Sciences pour le Vivant, F-38054 Grenoble, France; INRA, USC1359, 17 rue des Martyrs, F-38054 Grenoble, France; CNRS, Laboratoire de Physiologie Cellulaire & Végétale, UMR 5168, 17 rue des Martyrs, F-38054 Grenoble, France.
authors.forename: Michel
authors.initials: M
authors.lastname: Matringe
authors.affiliation: Kazan Institute of Biochemistry and Biophysics, Russian Academy of Sciences, P.O. Box 30, 420111 Kazan, Russia.
authors.forename: Alexander
authors.initials: A
authors.lastname: Grechkin
authors.affiliation: Univ. Grenoble Alpes, F-38054 Grenoble, France; Commissariat à l'Energie Atomique et aux Energies Alternatives, Direction des Sciences du Vivant, Institut de Recherches en Technologies et Sciences pour le Vivant, F-38054 Grenoble, France; INRA, USC1359, 17 rue des Martyrs, F-38054 Grenoble, France; CNRS, Laboratoire de Physiologie Cellulaire & Végétale, UMR 5168, 17 rue des Martyrs, F-38054 Grenoble, France.
authors.forename: Norbert
authors.initials: N
authors.lastname: Rolland
mesh_terms: D017360:Arabidopsis / Q000737:chemistry; D029681:Arabidopsis Proteins / Q000378:metabolism; D002736:Chloroplasts / Q000378:metabolism*; D003517:Cyclopentanes / Q000378:metabolism; D005231:Fatty Acids, Unsaturated; D008084:Lipoxygenase / Q000378:metabolism; D008563:Membrane Lipids / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism; D010084:Oxidation-Reduction; D054883:Oxylipins / Q000378:metabolism; D011808:Quinone Reductases / Q000378:metabolism*; D011809:Quinones / Q000378:metabolism
chemical_list: D029681:Arabidopsis Proteins; D003517:Cyclopentanes; D005231:Fatty Acids, Unsaturated; D008563:Membrane Lipids; D008565:Membrane Proteins; D054883:Oxylipins; D011809:Quinones; C025999:12-oxophytodienoic acid; C011006:jasmonic acid; C117433:13-lipoxygenase; D008084:Lipoxygenase; D011808:Quinone Reductases
keywords: Alkenone reductase; Chloroplast; Jasmonate; Oxylipin; Reactive electrophile species; γ-Ketols