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Cell. 1994 Jan 28;76(2):393-402.

Molecular characterization of a copper transport protein in S. cerevisiae: an unexpected role for copper in iron transport.

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Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health Bethesda, Maryland 20892.


We report the identification and characterization of CTR1, a gene in the yeast S. cerevisiae that encodes a multispanning plasma membrane protein specifically required for high affinity copper transport into the cell. The predicted protein contains a methionine- and serine-rich domain that includes 11 examples of the sequence Met-X2-Met, a motif noted in proteins involved in bacterial copper metabolism. CTR1 mutants and deletion strains have profound deficiency in ferrous iron uptake, thus revealing a requirement for copper in mediating ferrous transport into the cell. Genetic evidence suggests that the target for this requirement is the FET3 gene (detailed in a companion study), predicted to encode a copper-containing protein that acts as a cytosolic ferro-oxidase. These findings provide an unexpected mechanistic link between the uptake of copper and iron.

[Indexed for MEDLINE]

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