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J. Biol. Chem., Vol. 276, Issue 36, 33730-33735, September 7, 2001
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From the School of Life and Environmental Sciences, University of
Nottingham, University Park, Nottingham NG7 2RD, United Kingdom
The GPX1, GPX2, and
GPX3 genes of Saccharomyces cerevisiae
have been reported previously to encode glutathione peroxidases (GPxs).
We re-examined the sequence alignments of these proteins with GPxs from
higher eukaryotes. Sequence identities, particularly with phospholipid
hydroperoxide glutathione peroxidases (PHGPxs), were enhanced
markedly by introduction to the yeast sequences of gaps that are
characteristic of PHGPxs. PHGPx-like activity was detectable in
extracts from wild-type S. cerevisiae and was diminished in
extracts from gpx1
, gpx2, and
gpx3 deletion mutants; PHGPx activity was almost absent
in a gpx1/gpx2/gpx3 triple mutant. Studies with cloned GPX1, GPX2, and
GPX3 expressed heterologously in Escherichia
coli confirmed that these genes encode proteins with PHGPx
activity. An S. cerevisiae
gpx1/gpx2/gpx3 mutant was
defective for growth in medium supplemented with the
oxidation-sensitive polyunsaturated fatty acid linolenate (18:3). This
sensitivity to 18:3 was more marked than sensitivity to
H2O2. Unlike
H2O2 toxicity, delayed toxicity of 18:3 toward
gpx1/gpx2/gpx3 cells was
correlated with the gradual incorporation of 18:3 into S. cerevisiae membrane lipids and was suppressible with
-tocopherol, an inhibitor of lipid peroxidation. The results show
that the GPX genes of S. cerevisiae, previously
reported to encode GPxs, encode PHGPxs (PHGPx1, PHGPx2, and PHGPx3) and
that these enzymes protect yeast against phospholipid hydroperoxides as
well as nonphospholipid peroxides during oxidative stress. This
is the first report of an organism that expresses PHGPx from more than
one gene and produces PHGPx in the absence of a GPx.
To whom correspondence should be addressed. Tel.: 44-115-9513315;
Fax: 44-115-9513251; E-mail: Simon.Avery@nottingham.ac.uk.
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