Abstract
Intracellular levels of iron are tightly regulated. Saccharomyces cerevisiae uses well-defined pathways to extract iron molecules from the environment. Once inside the cell, the iron molecules must be transferred to target sites via an intracellular iron transporter. Although analogous carriers have been described for other metals, such as copper, an iron transporter has yet to be identified. We used two-dimensional gel electrophoresis and mass spectrometry techniques to attempt to identify the iron transporter from cytosolic fraction of S. cerevisiae. In this study, we identified the iron-binding activity of thioredoxin reductase, and our data suggest a potential role for this enzyme in intracellular iron transport.
Original language | English |
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Pages (from-to) | 63-68 |
Number of pages | 6 |
Journal | Biochemical and biophysical research communications |
Volume | 371 |
Issue number | 1 |
DOIs | |
Publication status | Published - 2008 Jun 20 |
Bibliographical note
Funding Information:This work was supported by the Korea Research Foundation Grant funded by the Korean Government (MOEHRD, Basic Research Promotion Fund) (KRF-2007-313-C00456).
Keywords
- 2-DE
- IMAC
- Iron
- Saccharomyces cerevisiae
- Thioredoxin reductase
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology