The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake.
Abstract
S. cerevisiae accumulate iron by a process requiring a ferrireductase and a ferrous transporter. We have isolated a mutant, fet3, defective for high affinity Fe(II) uptake. The wild-type FET3 gene was isolated by complementation of the mutant defect. Sequence analysis of the gene revealed the presence of an open reading frame coding for a protein with strong similarity to the family of blue multicopper oxidoreductases. Consistent with the role of copper in iron transport, growth of wild-type cells in copper-deficient media resulted in decreased ferrous iron transport. Addition of copper, but not other transition metals (manganese or zinc), to the assay media resulted in the recovery of Fe(II) transporter activity. We suggest that the catalytic activity of the Fet3 protein is required for cellular iron accumulation.
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In yeast, the ferrous iron permease FTR1 requires the multicopper ferroxidase FET3 for correct localization on the cell surface.
“This situation is somewhat analogous to iron transport in yeast, where the ferrous iron permease FTR1 (functionally analogous but structurally unrelated to DMT1) requires the multicopper ferroxidase FET3 for correct localization on the cell surface.85,86”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [85]
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- Authors
- Askwith, C., Eide, D., Van Ho, A., Bernard, P. S., Li, L., Davis-Kaplan, S., Sipe, D. M., & Kaplan, J.
- Affiliations
- University of Utah (US)
- University of Minnesota (US)
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1994-01
- Volume
- 76
- Issue
- 2
- Pages
- 403-410
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W1969060808
- Cited by
- 670
- References
- 39
- Citations by year
- 2026: 6 · 2025: 12 · 2024: 5 · 2023: 8 · 2022: 13 · 2021: 21 · 2020: 18 · 2019: 5 · 2018: 11 · 2017: 13 · 2016: 7 · 2015: 8 · 2014: 16 · 2013: 13 · 2012: 19
- FWCI
- 24.00
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r29gm048139-04)
- National Institute of General Medical Sciences (GM 48139)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK 5-30534, T32 DK07115-16, T32DK007115)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Keywords
- multicopper oxidase, ferrous iron uptake, iron transport, Saccharomyces cerevisiae, ferrireductase, iron accumulation, copper deficiency
- MeSH terms
- Amino Acid Sequence, Biological Transport, Active, Ceruloplasmin, Cloning, Molecular, Ferrous Compounds, Genes, Fungal, Genetic Complementation Test, Iron, Metalloproteins, Molecular Sequence Data, Oxidoreductases, RNA, Messenger, Saccharomyces cerevisiae, Gene Expression Regulation, Fungal, Mutagenesis, Insertional, Sequence Alignment, Sequence Homology, Amino Acid, Saccharomyces cerevisiae Proteins
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