A novel role for thioredoxin reductase in the iron metabolism of S. cerevisiae

Biochem Biophys Res Commun. 2008 Jun 20;371(1):63-8. doi: 10.1016/j.bbrc.2008.03.156. Epub 2008 Apr 10.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Chromatography, Affinity / methods
  • Circular Dichroism
  • Culture Media
  • Iron / metabolism*
  • Iron-Binding Proteins / genetics
  • Iron-Binding Proteins / isolation & purification
  • Iron-Binding Proteins / physiology*
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / growth & development
  • Spectrophotometry, Ultraviolet
  • Thioredoxin Reductase 1 / genetics
  • Thioredoxin Reductase 1 / isolation & purification
  • Thioredoxin Reductase 1 / physiology*

Substances

  • Culture Media
  • Iron-Binding Proteins
  • Iron
  • Thioredoxin Reductase 1