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Simon Gudin

Study of the copper ATPase Ccc2 of Saccharomyces cerevisiae. From localization to function

Published on 13 November 2008


Thesis presented November 13, 2008

Abstract:
This thesis investigated two aspects of Ccc2, S. Cerevisiae copper ATPase. One is cellular and concerns the localization and the cellular function of Ccc2; the second one is biochemical and deals with the mechanism of copper transport by Ccc2. We found out that Ccc2 localizes at all the secretory pathway compartments and at the membrane of the ​vacuole. The latter result is the first evidence for a new function of Ccc2, that is to store copper into the vacuole lumen. Ccc2 is the first copper active transporter found in a vacuole. Our biochemical study shows that 2 coppers atoms bind to the isolated nucleotide domain of Ccc2. Two cysteines, C708 and C718, were identify as being part of the copper binding sites. Further studies will determine the function of these copper binding sites in the mechanism of copper transport by Ccc2.

Keywords:
Copper, Saccharomyces cerevisiae, ATPase Ccc2, intracellular traffic

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