Cm. Grant, Role of the glutathione/glutaredoxin and thioredoxin systems in yeast growth and response to stress conditions, MOL MICROB, 39(3), 2001, pp. 533-541
Sulphydryl groups (-SH) play a remarkably broad range of roles in the cell,
and the redox status of cysteine residues can affect both the structure an
d the function of numerous enzymes, receptors and transcription factors. Th
e intracellular milieu is usually a reducing environment as a result of hig
h concentrations of the low-molecular-weight thiol glutathione (GSH). Howev
er, reactive oxygen species (ROS), which are the products of normal aerobic
metabolism, as well as naturally occurring free radical-generating compoun
ds, can alter this redox balance. A number of cellular factors have been im
plicated in the regulation of redox homeostasis, including the glutathione/
glutaredoxin and thioredoxin systems. Glutaredoxins and thioredoxins are ub
iquitous small heat-stable oxidoreductases that have proposed functions in
many cellular processes, including deoxyribonucleotide synthesis, repair of
oxidatively damaged proteins, protein folding and sulphur metabolism. This
review describes recent findings in the lower eukaryote Saccharomyces cere
visiae that are leading to a better understanding of their role in redox ho
meostasis in eukaryotic cell metabolism.