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J Biol Chem, Vol. 274, Issue 53, 38061-38070, December 31, 1999
From the Department of Physiology and Biophysics University of
Iowa, Iowa City, Iowa 52242
Iron transport across the plasma membrane appears
to be a unidirectional process whereby iron uptake is essentially
irreversible. One of the major sequestration sites for iron is the
vacuole that stores a variety of metals, either as a mechanism to
detoxify the cell or as a reservoir of metal to enable the cell to grow when challenged by a low iron environment. Exactly how the vacuole contributes to the overall iron metabolism of the cell is unclear because mutations that affect vacuolar function also perturb the assembly of the plasma membrane high affinity transport system composed
of a copper-containing iron oxidase, Fet3p, and an
Fe3+-specific iron transporter, Ftr1p. Here, we
characterize the iron transporter homologue Fth1p, which is similar to
the high affinity plasma membrane iron transporter Ftr1p. We found that
Fth1p was localized to the vacuolar surface and, like other proteins
that function on the vacuole, did not undergo Pep4-dependent
degradation. Co-immunoprecipitation experiments showed that Fth1p also
associates with the Fet3p oxidase homologue, Fet5p; and disruption of
the FET5 gene results in the accumulation of Fth1p in the
endoplasmic reticulum. We also found that loss of this protein complex
leads to elevated transcriptional activity of the FET3 gene
and compromises the ability of the cell to switch from fermentative
metabolism to respiratory metabolism. Because the Fet5 protein is
oriented such that the oxidase domain of Fet5p is lumenal, this complex may be responsible for mobilizing intravacuolar stores of iron.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF177330.
The Iron Transporter Fth1p Forms a Complex with the Fet5 Iron
Oxidase and Resides on the Vacuolar Membrane*
*
This work was supported by a grant from the National
Institutes of Health (RO1 GM58202-01) and by a pilot grant from the
Diabetes Endocrinology Research Center (DK25295).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Physiology
and Biophysics, Rm. 5-660, Bowen Science Bldg., University of Iowa,
Iowa City, IA 52242. Tel.: 319-335-7842; Fax: 319-335-7330.
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