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HMA1 was identified in the envelope of the chloroplast by proteomics. The localization is confirmed by fractionation experiments and GFP-fusions. HMA1 mediates Cu and Zn transport when expressed in yeast. hma1 insertion mutants show a light-sensitive phenotype, and have reduced plastid SOD activity and Cu content in the chloroplast, but have normal plastocyanin levels.
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Seigneurin-Berny D., Gravot A., Auroy P., Mazard C., Kraut A., Finazzi G., Grunwald D., Rappaport F., Vavasseur A., Joyard J., et al. HMA1, a new Cu-ATPase of the chloroplast envelope, is essential for growth under adverse light conditions. J Biol Chem 281 (2006) 2882-2892. HMA1 was identified in the envelope of the chloroplast by proteomics. The localization is confirmed by fractionation experiments and GFP-fusions. HMA1 mediates Cu and Zn transport when expressed in yeast. hma1 insertion mutants show a light-sensitive phenotype, and have reduced plastid SOD activity and Cu content in the chloroplast, but have normal plastocyanin levels.
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The Arabidopsis thaliana CUTA gene encodes an evolutionarily conserved copper binding chloroplast protein
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Burkhead J., Abdel-Ghany S., Morrill J., Pilon-Smits E.A.H., and Pilon M. The Arabidopsis thaliana CUTA gene encodes an evolutionarily conserved copper binding chloroplast protein. Plant J 34 (2003) 856-867
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The unusually stable quaternary structure of human Cu/Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status
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Arnesano F., Banci L., Bertini I., Martinelli M., Furukawa Y., and O'Halloran T.V. The unusually stable quaternary structure of human Cu/Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status. J Biol Chem 279 (2004) 47998-48003
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AtCCS is a functional homolog of the yeast copper chaperone Ccs1/Lys7
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Abdel-Ghany S.E., Burkhead J.L., Gogolin K.A., Andres-Colas N., Bodecker J.R., Puig S., Penarrubia L., and Pilon M. AtCCS is a functional homolog of the yeast copper chaperone Ccs1/Lys7. FEBS Lett 579 (2005) 2307-2312
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A copper chaperone for superoxide dismutase that confers three types of copper/zinc superoxide dismutase activity in Arabidopsis
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A T-DNA mutant for the Arabidopsis CCS gene was obtained and analyzed. The mutation effects the activation of Cu/ZnSOD in the cytosol, in the chloroplast stroma and in the peroxisomes. Using a complementation approach, the authors show that the amino-terminal ATX-like domain is required for CCS function and that the delivery of Cu to plastid Cu/ZnSOD requires CSS with an intact plastid-targeting sequence.
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Chu C.C., Lee W.C., Guo W.Y., Pan S.M., Chen L.J., Li H.M., and Jinn T.L. A copper chaperone for superoxide dismutase that confers three types of copper/zinc superoxide dismutase activity in Arabidopsis. Plant Physiol 139 (2005) 425-436. A T-DNA mutant for the Arabidopsis CCS gene was obtained and analyzed. The mutation effects the activation of Cu/ZnSOD in the cytosol, in the chloroplast stroma and in the peroxisomes. Using a complementation approach, the authors show that the amino-terminal ATX-like domain is required for CCS function and that the delivery of Cu to plastid Cu/ZnSOD requires CSS with an intact plastid-targeting sequence.
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Plant Physiol
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Chu, C.C.1
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Rizhsky L., Liang H., and Mittler R. The water-water cycle is essential for chloroplast protection in the absence of stress. J Biol Chem 278 (2003) 38921-38925
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Jensen L.T., and Culotta V.C. Activation of Cu/Zn superoxide dismutases from C. elegans does not require the copper chaperone CCS. J Biol Chem 280 (2005) 41373-41379
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Eriksson M., Moseley J.L., Tottey S., del Campo J.A., Quinn J., Kim Y., and Merchant S. Molecular genetic dissection of nutritional copper signalling in Chlamydomonas distinguishes regulatory and target genes. Genetics 168 (2004) 795-807
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Chimeras of P1-type ATPases and their transcriptional regulators: contributions of a cytosolic amino-terminal domain to metal specificity
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The authors demonstrate that the amino-terminal domains of the cyanobacterial heavy-metal Ptype ATPases contribute to metal specificity. However, Cu can interact even more strongly than Zn with the amino-terminal domain of the Zn transporter. Therefore, Cu could displace Zn from its own transporter. This interaction might be prevented in vivo by the presence of the ATX Cu chaperone, which sequesters Cu but can interact only with the Cu-specific transporters and not with the Zn transporter.
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Borrelly G.P.M., Rondet S.A.M., Tottey S., and Robinson N.J. Chimeras of P1-type ATPases and their transcriptional regulators: contributions of a cytosolic amino-terminal domain to metal specificity. Mol Microbiol 53 (2004) 217-227. The authors demonstrate that the amino-terminal domains of the cyanobacterial heavy-metal Ptype ATPases contribute to metal specificity. However, Cu can interact even more strongly than Zn with the amino-terminal domain of the Zn transporter. Therefore, Cu could displace Zn from its own transporter. This interaction might be prevented in vivo by the presence of the ATX Cu chaperone, which sequesters Cu but can interact only with the Cu-specific transporters and not with the Zn transporter.
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Mol Microbiol
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Banci L., Bertini I., Ciofi-Baffoni S., Su X.C., Borrelly G.P., and Robinson N.J. Solution structures of a cyanobacterial metallochaperone: insight into an atypical copper-binding motif. J Biol Chem 279 (2004) 27502-27510
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Banci, L.1
Bertini, I.2
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Su, X.C.4
Borrelly, G.P.5
Robinson, N.J.6
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