tailieunhanh - Báo cáo khoa học: Dissecting the role of the N-terminal metal-binding domains in activating the yeast copper ATPase in vivo

In yeast, copper delivery to the trans-Golgi network involves interactions between the metallo-chaperone Atx1 and the N-terminus of Ccc2, the P-type ATPase responsible for copper transport acrosstrans-Golgi network membranes. Disruption of the Atx1–Ccc2 route leads to cell growth arrest in a copper-and-iron-limited medium, a phenotype allowing complementa-tion studies. | ỊFEBS Journal Dissecting the role of the N-terminal metal-binding domains in activating the yeast copper ATPase in vivo Isabelle Morin1 2 3 Simon Gudin1 2 3 Elisabeth Mintz1 2 3 and Martine Cuillel1 2 3 1 CEA DSV iRTSV Laboratoire de Chimie et Biologie des Metaux Grenoble France 2 CNRS UMR 5249 Grenoble France 3 Universite Joseph Fourier Grenoble France Keywords Atx1 Ccc2 complementation Cu I domain-domain interactions Correspondence M. Cuillel Cea iRTSV LCBM 17 rue des Martyrs 38054 Grenoble Cedex 9 France Fax 334 38 78 54 87 Tel 334 38 78 96 51 E-mail Present address Comparative Genomics Centre James Cook University Townsville Australia Received 24 March 2009 revised 28 May 2009 accepted 16 June 2009 doi In yeast copper delivery to the trans-Golgi network involves interactions between the metallo-chaperone Atx1 and the N-terminus of Ccc2 the P-type ATPase responsible for copper transport across trans-Golgi network membranes. Disruption of the Atx1-Ccc2 route leads to cell growth arrest in a copper-and-iron-limited medium a phenotype allowing complementation studies. Coexpression of Atx1 and Ccc2 mutants in an atx1Accc2A strain allowed us to study in vivo Atx1-Ccc2 and intra-Ccc2 domaindomain interactions leading to active copper transfer into the trans-Golgi network. The Ccc2 N-terminus encloses two copper-binding domains M1 and M2. We show that in vivo Atx1-M1 or Atx1-M2 interactions activate Ccc2. M1 or M2 expressed in place of the metallo-chaperone Atx1 were not as efficient as Atx1 in delivering copper to the Ccc2 N-terminus. However when the Ccc2 N-terminus was truncated these independent metalbinding domains behaved like functional metallo-chaperones in delivering copper to another copper-binding site in Ccc2 whose identity is still unknown. Therefore we provide evidence of a dual role for the Ccc2 N-terminus namely to receive copper from Atx1 and to convey copper to another domain of Ccc2 thereby .

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