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Vol. 9, Issue 5, 1081-1091, May 1998
Cooperative Research Center for Food Industry Innovation, School of
Biochemistry and Molecular Genetics, University of New South Wales,
Sydney, New South Wales 2052, Australia
Glutaredoxins are small heat-stable proteins that act as
glutathione-dependent disulfide oxidoreductases. Two genes, designated GRX1 and GRX2, which share 40-52%
identity and 61-76% similarity with glutaredoxins from bacterial and
mammalian species, were identified in the yeast Saccharomyces
cerevisiae. Strains deleted for both GRX1 and
GRX2 were viable but lacked heat-stable oxidoreductase activity using 
-hydroxyethylene disulfide as a substrate.
Surprisingly, despite the high degree of homology between Grx1 and Grx2
(64% identity), the grx1 mutant was unaffected in
oxidoreductase activity, whereas the grx2 mutant
displayed only 20% of the wild-type activity, indicating that Grx2
accounted for the majority of this activity in vivo. Expression
analysis indicated that this difference in activity did not arise as a
result of differential expression of GRX1 and
GRX2. In addition, a grx1 mutant was
sensitive to oxidative stress induced by the superoxide anion, whereas
a strain that lacked GRX2 was sensitive to hydrogen
peroxide. Sensitivity to oxidative stress was not attributable to
altered glutathione metabolism or cellular redox state, which did not
vary between these strains. The expression of both genes was similarly
elevated under various stress conditions, including oxidative, osmotic, heat, and stationary phase growth. Thus, Grx1 and Grx2 function differently in the cell, and we suggest that glutaredoxins may act as
one of the primary defenses against mixed disulfides formed following
oxidative damage to proteins.
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