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Characterization of the recombinant copper chaperone (CCS) from the plant Glycine (G.) max.

AuthorsSagasti Escalona, Sara ; Yruela Guerrero, Inmaculada ; Bernal Ibáñez, María ; Luján Serrano, María Ángeles ; Frago, Susana; Medina, Milagros; Picorel Castaño, Rafael
Issue Date2011
PublisherRoyal Society of Chemistry (UK)
CitationSagasti S, Yruela I, Bernal M, Lujan MA, Frago S, Medina M, Picorel R. Characterization of the recombinant copper chaperone (CCS) from the plant Glycine (G.) max. Metallomics 3 (2): 169-175 (2011)
AbstractThe goal of the present work was to characterize the recombinant copper chaperone (CCS) from soybean. Very little is known about plant copper chaperones, which makes this study of current interest, and allows for a comparison with the better known homologues from yeast and humans. To obtain sizeable amounts of pure protein suitable for spectroscopic characterization, we cloned and overexpressed the G. max CCS chaperone in E. coli in the presence of 0.5 mM CuSO4 and 0.5 mM ZnSO4 in the broth. A pure protein preparation was obtained by using two IMAC steps and pH gradient chromatography. Most of the proteins were obtained as apo-form, devoid of copper atoms. The chaperone showed a high content (i.e., over 40%) of loops, turns and random coil as determined both by circular dichroism and homology modelling. The homology 3-D structural model suggests the protein might fold in three structural protein domains. The 3-D model along with the primary structure and spectroscopic data may suggest that copper atoms occupy the two metal binding sites, MKCEGC and CTC, within the N-terminal domain I and C-terminal domain III, respectively. But only one Zn-binding site was obtained spectroscopically.
Description31 Pag, Figs. The definitive version is available at: http://pubs.rsc.org/en/Journals/Journal/MT
Publisher version (URL)http://dx.doi.org/10.1039/C0MT00055H
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