A novel role for thioredoxin reductase in the iron metabolism of S. cerevisiae.
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.
Kang
Hyun-Jun
HJ
School of Life Sciences and Biotechnology, Korea University, Anam-dong, Sungbuk-gu, Seoul 136-713, Republic of Korea.
Choi
So-Woong
SW
Heo
Dong-Hyuk
DH
Jeong
Mi-Young
MY
Sung
Ha-Chin
HC
Yun
Cheol-Won
CW
D002846:Chromatography, Affinity / Q000379:methods; D002942:Circular Dichroism; D003470:Culture Media; D007501:Iron / Q000378:metabolism*; D033862:Iron-Binding Proteins / Q000235:genetics / Q000302:isolation & purification / Q000502:physiology*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development; D013056:Spectrophotometry, Ultraviolet; D054481:Thioredoxin Reductase 1 / Q000235:genetics / Q000302:isolation & purification / Q000502:physiology*
D003470:Culture Media; D033862:Iron-Binding Proteins; D007501:Iron; D054481:Thioredoxin Reductase 1