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J. Biol. Chem., Vol. 276, Issue 5, 3555-3563, February 2, 2001
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From the Department of Cell and Molecular Biology, Microbiology,
Göteborg University, Box 463, SE 40530 Göteborg, Sweden
We have characterized the strongly
homologous GPP1/RHR2 and GPP2/HOR2 genes,
encoding isoforms of glycerol 3-phosphatase. Mutants lacking both
GPP1 and GPP2 are devoid of glycerol
3-phosphatase activity and produce only a small amount of glycerol,
confirming the essential role for this enzyme in glycerol biosynthesis.
Overproduction of Gpp1p and Gpp2p did not significantly enhance
glycerol production, indicating that glycerol phosphatase is not
rate-limiting for glycerol production. Previous studies have shown that
expression of both GPP1 and GPP2 is induced
under hyperosmotic stress and that induction partially depends on the
HOG (high osmolarity glycerol) pathway. We here show that expression of
GPP1 is strongly decreased in strains having low protein
kinase A activity, although it is still responsive to osmotic stress.
The gpp1
The Yeast Glycerol 3-Phosphatases Gpp1p and Gpp2p Are Required
for Glycerol Biosynthesis and Differentially Involved in the Cellular
Responses to Osmotic, Anaerobic, and Oxidative Stress*
/gpp2 double mutant is
hypersensitive to high osmolarity, whereas the single mutants remain
unaffected, indicating GPP1 and GPP2 substitute
well for each other. Transfer to anaerobic conditions does not affect
expression of GPP2, whereas GPP1 is transiently
induced, and mutants lacking GPP1 show poor anaerobic
growth. All gpp mutants show increased levels of glycerol
3-phosphate, which is especially pronounced when gpp1
and gpp1/gpp2 mutants are transferred to
anaerobic conditions. The addition of acetaldehyde, a strong oxidizer
of NADH, leads to decreased glycerol 3-phosphate levels and restored anaerobic growth of the gpp1/gpp2 mutant,
indicating that the anaerobic accumulation of NADH causes glycerol
3-phosphate to reach growth-inhibiting levels. We also found the
gpp1/gpp2 mutant is hypersensitive to the
superoxide anion generator, paraquat. Consistent with a role for
glycerol 3-phosphatase in protection against oxidative stress,
expression of GPP2 is induced in the presence of paraquat.
This induction was only marginally affected by the general
stress-response transcriptional factors Msn2p/4p or protein kinase A
activity. We conclude that glycerol metabolism plays multiple roles in
yeast adaptation to altered growth conditions, explaining the complex
regulation of glycerol biosynthesis genes.
*
This work was supported by grants from the Swedish Natural
Science Research Council and the Swedish Research Council for
Engineering Sciences, and by the European Commission (Contracts
BIO4-CT95-0161 and FMRX-CT95-0007).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Tel.: 46-31-773-2580;
Fax: 46-31-773-2599; E-mail: Lennart.Adler@gmm.gu.se.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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