Identification of Two Conserved Residues Involved in Copper Release from Chloroplast PIB-1-ATPases
| Autor: | Cécile Giustini, Emeline Sautron, Thuy Van Dang, Daniel Salvi, Patrice Catty, Lucas Moyet, Serge Crouzy, Norbert Rolland, Daphné Seigneurin-Berny |
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| Přispěvatelé: | Physiologie cellulaire et végétale (LPCV), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-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 de Chimie et Biologie des Métaux (LCBM - UMR 5249), Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat a l'Energie Atomique et aux Energies Alternatives, Centre National de la Recherche Scientifique, French National Institute for Agricultural Research, University of Grenoble Alpes, GRAL Labex [ANR-10-LABX-49-01], CEA, Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes (UGA)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Institut National de la Recherche Agronomique (INRA)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG) |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Saccharomyces cerevisiae Amino Acid Motifs Arabidopsis chemistry.chemical_element Plant Biology Biochemistry Chloroplast membrane Thylakoids 03 medical and health sciences chloroplast ATPase [SDV.BV]Life Sciences [q-bio]/Vegetal Biology Histidine [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Molecular Biology Plastocyanin Adenosine Triphosphatases 030102 biochemistry & molecular biology biology Arabidopsis Proteins food and beverages Cell Biology biology.organism_classification Copper release site Copper Recombinant Proteins Chloroplast Lactococcus lactis 030104 developmental biology chemistry PIB-1-ATPases Thylakoid plant biochemistry copper transport copper release site Thylakoid Membrane Proteins Cysteine |
| Zdroj: | Journal of Biological Chemistry Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2016, 291 (38), pp.20136-20148. ⟨10.1074/jbc.M115.706978⟩ Journal of Biological Chemistry 38 (291), 20136-20148. (2016) Journal of Biological Chemistry, 2016, 291 (38), pp.20136-20148. ⟨10.1074/jbc.M115.706978⟩ |
| ISSN: | 0021-9258 1083-351X |
| DOI: | 10.1074/jbc.M115.706978⟩ |
| Popis: | International audience; Copper is an essential transition metal for living organisms. In the plant model Arabidopsis thaliana, half of the copper content is localized in the chloroplast and, as a cofactor of plastocyanin, copper is essential for photosynthesis. Within the chloroplast, copper delivery to plastocyanin involves two transporters of the PIB-1-ATPases subfamily, HMA6 at the chloroplast envelope and HMA8, in the thylakoid membranes. Both proteins are high affinity copper transporters but share distinct enzymatic properties. In the present work, the comparison of 140 sequences of PIB-1-ATPases revealed a conserved region unusually rich in histidine and cysteine residues in the TMA-L1 region of eukaryotic chloroplast copper ATPases. To evaluate the role of these residues, we mutated them in HMA6 and HMA8. Mutants of interest were selected from phenotypic tests in yeast and produced in Lactococcus lactis for further biochemical characterizations using phosphorylation assays from ATP and Pi. Combining functional and structural data, we highlight the importance of the cysteine and the first histidine of the Cx3Hx2H motif in the process of copper release from HMA6 and HMA8, and propose a copper pathway through the membrane domain of these transporters. Finally our work suggests a more general role of the histidine residue in the transport of copper by PIB-1-ATPases. |
| Databáze: | OpenAIRE |
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