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

Cell. 1994 Jan 28;76(2):393-402. doi: 10.1016/0092-8674(94)90345-x.


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.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Biological Transport
  • Cation Transport Proteins*
  • Cloning, Molecular
  • Copper / metabolism*
  • Copper Transporter 1
  • Ferrous Compounds / metabolism
  • Fungal Proteins / genetics*
  • Fungal Proteins / metabolism
  • Genes, Fungal*
  • Iron / metabolism
  • Membrane Proteins / genetics*
  • Membrane Proteins / metabolism
  • Molecular Sequence Data
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae Proteins*
  • Sequence Alignment
  • Sequence Homology, Amino Acid


  • CTR1 protein, S cerevisiae
  • Cation Transport Proteins
  • Copper Transporter 1
  • Ferrous Compounds
  • Fungal Proteins
  • Membrane Proteins
  • Saccharomyces cerevisiae Proteins
  • Copper
  • Iron

Associated data

  • GENBANK/U02511