A Permease-Oxidase Complex Involved in High-Affinity Iron Uptake in Yeast
- 15 March 1996
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 271 (5255), 1552-1557
- https://doi.org/10.1126/science.271.5255.1552
Abstract
Iron must cross biological membranes to reach essential intracellular enzymes. Two proteins in the plasma membrane of yeast—a multicopper oxidase, encoded by the FET3 gene, and a permease, encoded by the FTR1 gene—were shown to mediate high-affinity iron uptake. FET3 expression was required for FTR1 protein to be transported to the plasma membrane. FTR1 expression was required for apo-FET3 protein to be loaded with copper and thus acquire oxidase activity. FTR1 protein also played a direct role in iron transport. Mutations in a conserved sequence motif of FTR1 specifically blocked iron transport.Keywords
This publication has 40 references indexed in Scilit:
- High Resolution Crystal Structures of Amphibian Red-Cell L Ferritin: Potential Roles for Structural Plasticity and Solvation in FunctionJournal of Molecular Biology, 1995
- A Cellular Stress Model for the Sequestration of Redox‐Active Glial Iron in the Aging and Degenerating Nervous SystemJournal of Neurochemistry, 1995
- A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humansNature Genetics, 1995
- The FET3 Gene Product Required for High Affinity Iron Transport in Yeast Is a Cell Surface FerroxidaseJournal of Biological Chemistry, 1995
- The Role of the L-Chain in Ferritin Iron IncorporationJournal of Molecular Biology, 1994
- The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptakeCell, 1994
- Isolation and Characterization of a Human Liver cDNA as a Candidate Gene for Wilson DiseaseBiochemical and Biophysical Research Communications, 1993
- Basic local alignment search toolJournal of Molecular Biology, 1990
- Plants can utilize iron form Fe‐N,N'‐di‐(2‐hydroxybenzoyl)‐ethylenediamine‐N,N'‐diacetic acid, a ferric chelate with 106greater formation constant than Fe‐EDDHA.Journal of Plant Nutrition, 1988
- The role of ceruloplasmin in iron metabolismJournal of Clinical Investigation, 1970