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Ionic self-complementarity induces amyloid-like fibril formation in an isolated domain of a plant copper metallochaperone protein

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Ionic self-complementarity induces amyloid-like fibril formation in an isolated domain of a plant copper metallochaperone protein

dc.contributor.author	Mira Aparicio, Helena
dc.contributor.author	Vilar, Marçal
dc.contributor.author	Esteve, Vicent
dc.contributor.author	Martinell, Marc
dc.contributor.author	Kogan, Marcelo J.
dc.contributor.author	Giralt, Ernest
dc.contributor.author	Salom, David
dc.contributor.author	Mingarro Muñoz, Ismael
dc.contributor.author	Peñarrubia Blasco, Lola
dc.contributor.author	Pérez Payá, Enrique
dc.date.accessioned	2016-09-06T16:51:34Z
dc.date.available	2016-09-06T16:51:34Z
dc.date.issued	2004
dc.identifier.citation	Mira Aparicio, Helena Vilar, Marçal Esteve, Vicent Martinell, Marc Kogan, Marcelo J. Giralt, Ernest Salom, David Mingarro Muñoz, Ismael Peñarrubia Blasco, Lola Pérez Payá, Enrique 2004 Ionic self-complementarity induces amyloid-like fibril formation in an isolated domain of a plant copper metallochaperone protein Bmc Structural Biology 4 7 1 15
dc.identifier.uri	http://hdl.handle.net/10550/54927
dc.description.abstract	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 beta-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.
dc.language.iso	eng
dc.relation.ispartof	Bmc Structural Biology, 2004, vol. 4, num. 7, p. 1-15
dc.subject	Proteïnes
dc.subject	Bioquímica
dc.title	Ionic self-complementarity induces amyloid-like fibril formation in an isolated domain of a plant copper metallochaperone protein
dc.type	journal article	es_ES
dc.date.updated	2016-09-06T16:51:35Z
dc.identifier.doi	10.1186/1472-6807-4-7
dc.identifier.idgrec	008440
dc.rights.accessRights	open access	es_ES