English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/1422
Compartir / Impacto:
Estadísticas
Add this article to your Mendeley library MendeleyBASE
Ver citas en Google académico
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar otros formatos: Exportar EndNote (RIS)Exportar EndNote (RIS)Exportar EndNote (RIS)
Título : Ionic self-complementarity induces amyloid-like fibril formation in an isolated domain of a plant copper metallochaperone protein
Autor : Mira, Helena; Vilar, Marçal; Esteve, Vicent; Martinell, Marc; Kogan, Marcelo J.; Giralt, Ernest; Salom, David; Mingarro, Ismael; Peñarrubia, Lola; Pérez-Payá, Enrique
Fecha de publicación : 4-jun-2004
Editor: BioMed Central
Citación : BMC Structural Biology 2004, 4:7
Resumen: [Background] Arabidopsis thaliana copper metallochaperone CCH is a functional homologue of yeast antioxidant ATX1, involved in cytosolic copper transport. In higher plants, CCH has to be transported to specialised cells through plasmodesmata, being the only metallochaperone reported to date that leaves the cell where it is synthesised. CCH has two different domains, the N-terminal domain conserved among other copper-metallochaperones and a C-terminal domain absent in all the identified non-plant metallochaperones. The aim of the present study was the biochemical and biophysical characterisation of the C-terminal domain of the copper metallochaperone CCH.
[Results] The conformational behaviour of the isolated C-domain in solution is complex and implies the adoption of mixed conformations in different environments. The ionic self-complementary peptide KTEAETKTEAKVDAKADVE, derived from the C-domain of CCH, adopts and extended conformation in solution with a high content in β-sheet structure that induces a pH-dependent fibril formation. Freeze drying electron microscopy studies revealed the existence of well ordered amyloid-like fibrils in preparations from both the C-domain and its derivative peptide.
[Conclusion] A number of proteins related with copper homeostasis have a high tendency to form fibrils. The determinants for fibril formation, as well as the possible physiological role are not fully understood. Here we show that the plant exclusive C-domain of the copper metallochaperone CCH has conformational plasticity and forms fibrils at defined experimental conditions. The putative influence of these properties with plant copper delivery will be addressed in the future.
Descripción : This article is available from: http://www.biomedcentral.com/1472-6807/4/7
URI : http://hdl.handle.net/10261/1422
ISSN: 1472-6807
Aparece en las colecciones: (IBV) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
1472-6807-4-7.pdf1,38 MBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.