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