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J Biol Chem, Vol. 274, Issue 38, 27002-27009, September 17, 1999
From the Research Institute for Food Science, Kyoto University,
Uji, Kyoto 611-0011, Japan
Three glutathione peroxidase homologs
(YKL026C, YBR244W, and
YIR037W/HYR1) were found in the
Saccharomyces Genome Database. We named them
GPX1, GPX2, and GPX3, respectively,
and we investigated the function of each gene product. The
gpx3
mutant was hypersensitive to peroxides, whereas
null mutants of the GPX1 and GPX2 did not show
any obvious phenotypes. Glutathione peroxidase activity decreased approximately 57 and 93% in the gpx3 and
gpx1/gpx2/gpx3 mutants, respectively, compared with that of wild type. Expression of the GPX3 gene was not induced by any stresses tested, whereas
that of the GPX1 gene was induced by glucose starvation.
The GPX2 gene expression was induced by oxidative stress,
which was dependent upon the Yap1p. The TSA1
(thiol-specific antioxidant) gene encodes thioredoxin peroxidase that
can reduce peroxides by using thioredoxin as a reducing power.
Disruption of the TSA1 gene enhanced the basal expression
level of the Yap1p target genes such as GSH1, GLR1, and GPX2 and that resulted in increases
of total glutathione level and activities of glutathione reductase and
glutathione peroxidase. However, expression of the TSA1
gene did not increase in the
gpx1/gpx2/gpx3 mutant.
Therefore, de novo synthesis and recycling of glutathione
were increased in the tsa1 mutant to maintain the
catalytic cycle of glutathione peroxidase reaction efficiently as a
backup system for thioredoxin peroxidase.
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