1. HMA1, a new Cu-ATPase of the chloroplast envelope, is essential for growth under adverse light conditions
- Author
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Daphné Seigneurin-Berny, Pierre Richaud, Giovanni Finazzi, Norbert Rolland, Antoine Gravot, Alexandra Kraut, Christophe Mazard, Pascaline Auroy, Jacques Joyard, Didier Grunwald, Fabrice Rappaport, Alain Vavasseur, Roux-Buisson, Nathalie, Laboratoire de physiologie cellulaire végétale (LPCV), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Laboratoire des Echanges Membranaires et Signalisation (LEMS), Université de la Méditerranée - Aix-Marseille 2-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Physiologie membranaire et moléculaire du chloroplaste (PMMC), Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), ANTE-INSERM U836, équipe 4, Muscles et pathologies, Laboratoire Canaux Ioniques, Fonctions et Pathologies, EMI 9931 CEA/INSERM/Universite' Joseph Fourier-DRDC/ CEA-Grenoble-EMI 9931 CEA/INSERM/Universite' Joseph Fourier-DRDC/ CEA-Grenoble, This work was supported by CNRS and CEA (Toxicologie Nucléaire Environnementale) research programs., Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC), and Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)
- Subjects
0106 biological sciences ,enveloppe chloroplastique ,Chloroplasts ,Light ,ATPase ,Mutant ,Arabidopsis ,MESH: Amino Acid Sequence ,[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC] ,01 natural sciences ,Biochemistry ,Chloroplast membrane ,protéine transmembranaire ,Yeasts ,Homeostasis ,MESH: Arabidopsis ,Cloning, Molecular ,Plastocyanin ,Cation Transport Proteins ,MESH: Superoxide Dismutase ,Plant Proteins ,Adenosine Triphosphatases ,0303 health sciences ,chloroplaste ,biology ,MESH: Plant Proteins ,ion métallique ,MESH: Yeasts ,zinc ,stress lumineux ,food and beverages ,Chloroplast ,MESH: Copper ,cuivre ,Chloroplast DNA ,plante expérimentale ,MESH: Homeostasis ,Copper-transporting ATPases ,MESH: Mutation ,Nuclear Envelope ,Molecular Sequence Data ,MESH: Arabidopsis Proteins ,[SDV.BC]Life Sciences [q-bio]/Cellular Biology ,TRANSPORT INTRACELLULLAIRE ,03 medical and health sciences ,MESH: Nuclear Envelope ,MESH: Cation Transport Proteins ,[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC] ,MESH: Adenosine Triphosphatases ,MESH: Cloning, Molecular ,Amino Acid Sequence ,Molecular Biology ,[SDV.BC] Life Sciences [q-bio]/Cellular Biology ,homéostasie ,030304 developmental biology ,Ion Transport ,MESH: Molecular Sequence Data ,MESH: Chloroplasts ,Arabidopsis Proteins ,Superoxide Dismutase ,arabidopsis thaliana ,Cell Biology ,biology.organism_classification ,MESH: Light ,MESH: Ion Transport ,Copper-Transporting ATPases ,Mutation ,biology.protein ,Copper ,010606 plant biology & botany - Abstract
International audience; Although ions play important roles in the cell and chloroplast metabolism, little is known about ion transport across the chloroplast envelope. Using a proteomic approach specifically targeted to the Arabidopsis chloroplast envelope, we have identified HMA1, which belongs to the metal-transporting P1B-type ATPases family. HMA1 is mainly expressed in green tissues, and we validated its chloroplast envelope localization. Yeast expression experiments demonstrated that HMA1 is involved in copper homeostasis and that deletion of its N-terminal His-domain partially affects the metal transport. Characterization of hma1 Arabidopsis mutants revealed a lower chloroplast copper content and a diminution of the total chloroplast superoxide dismutase activity. No effect was observed on the plastocyanin content in these lines. The hma1 insertional mutants grew like WT plants in standard condition but presented a photosensitivity phenotype under high light. Finally, direct biochemical ATPase assays performed on purified chloroplast envelope membranes showed that the ATPase activity of HMA1 is specifically stimulated by copper. Our results demonstrate that HMA1 offers an additional way to the previously characterized chloroplast envelope Cu-ATPase PAA1 to import copper in the chloroplast.
- Published
- 2006
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