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RESEARCH PRODUCT
Functional and conformational properties of the exclusive C-domain from the Arabidopsis copper chaperone (CCH)
Helena Mira AparicioMarçal VilarEnrique Pérez PayáLola Peñarrubia Blascosubject
endocrine systemMetallochaperone; Extended structure; Protein domainProtein domain:CIENCIAS DE LA VIDA::Bioquímica [UNESCO]MetallochaperoneUNESCO::CIENCIAS DE LA VIDA::BioquímicaCell BiologyMolecular BiologyBiochemistryExtended structuredescription
The Arabidopsis thaliana copper chaperone (CCH) is a small copper binding protein involved in copper trafficking. When compared to homologues from other eukaryotes, CCH has two different domains; the conserved N-domain and the plant-exclusive C-domain, a C-terminal extension with an unusual amino-acid composition. In order to characterize this extra C-domain, the CCH protein, the N-domain and the C-domain were all expressed separately in heterologous systems. While the N-domain retained the copper chaperone and antioxidant properties described for the yeast Atx1 and human HAH1 counterparts, the C-domain displayed particular structural properties that would be necessary to optimize copper homoeostasis in plant cells where it could be responsible for the metallochaperone plant-exclusive intercellular transport. The whole CCH protein and the C-domain, but not the N-domain, displayed altered SDS/PAGE mobilities. CD spectroscopy showed that the N-domain fold is representative of an a/b protein, while the C-domain adopts an extended conformation. mira@uv.es; mvilar@uv.es; paya@uv.es; penarrub@uv.es
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2001-07-09 |