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(Received for publication, September 30, 1994; and in revised form, November 9, 1994)
The yeast FET3 gene is required for high affinity iron
transport (Askwith, C., Eide, D., Ho, A. V., Bernard, P. S., Li, L.,
Davis-Kaplan, S., Sipe, D. M., and Kaplan, J. (1994) Cell 76,
403-410). The gene has extensive sequence homology to the family
of multi-copper oxidases. In this communication, we demonstrate that
the gene product is a cell surface ferroxidase involved in iron
transport. Cells that contain a functional FET3 gene product
exhibited an iron-dependent non-mitochondrial increase in oxygen
consumption. Comparison of the rate of iron oxidation to O
consumption yielded an approximate value of 4:1, as predicted for
a ferroxidase. Spheroplasts obtained from cells grown under low iron
conditions also displayed an iron-dependent increase in O consumption. Treatment of spheroplasts with trypsin or
affinity-purified antibodies directed against the putative external
ferroxidase domain of Fet3 had no effect on basal O consumption but inhibited the iron-dependent increase in O consumption. Anti-peptide antibodies directed against the
cytosolic domain of Fet3 had no effect on O consumption.
These studies indicate that Fet3 is a plasma membrane ferroxidase
required for high affinity iron uptake, in which the
ferroxidase-containing domain is localized on the external cell
surface.
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