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Studies of Cytochrome c Oxidase-Driven H+-Coupled Phosphate Transport Catalyzed by the Saccharomyces cerevisiae Pho84 Permease in Coreconstituted Vesicles

By Ulrika Fristedt, Michel van der Rest, Bert Poolman, Wil N. Konings and Bengt L. Persson


The proton-coupled Pho84 phosphate permease of Saccharomyces cerevisiae, overexpressed as a histidine-tagged chimera in Escherichia coli, was detergent-solubilized, purified, and reconstituted into proteoliposomes. Proteoliposomes containing the Pho84 protein were fused with proteoliposomes containing purified cytochrome c oxidase from beef heart mitochondria. Both components of the coreconstituted system were functionally incorporated in tightly sealed membrane vesicles in which the cytochrome c oxidase-generated electrochemical proton gradient could drive phosphate transport via the proton-coupled Pho84 permease. The metal dependency of transport indicates that a metal-phosphate complex is the translocated substrate.

Year: 1999
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