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HMA1, a new Cu-ATPase of the chloroplast envelope, is essential for growth under adverse light conditions

Authors :
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)
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)
Source :
Journal of Biological Chemistry, Journal of Biological Chemistry, 2006, 281 (5), pp.2882-92. ⟨10.1074/jbc.M508333200⟩, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2006, 281 (5), pp.2882-92. ⟨10.1074/jbc.M508333200⟩, Journal of Biological Chemistry 5 (281), 2882-2892. (2006)
Publication Year :
2006
Publisher :
HAL CCSD, 2006.

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.

Details

Language :
English
ISSN :
00219258 and 1083351X
Database :
OpenAIRE
Journal :
Journal of Biological Chemistry, Journal of Biological Chemistry, 2006, 281 (5), pp.2882-92. ⟨10.1074/jbc.M508333200⟩, Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2006, 281 (5), pp.2882-92. ⟨10.1074/jbc.M508333200⟩, Journal of Biological Chemistry 5 (281), 2882-2892. (2006)
Accession number :
edsair.doi.dedup.....74eb31300f41ea5aab8dbc5f1c7aaa47