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(Received for publication, July 16, 1996)
From the In Saccharomyces cerevisiae, loss of
cytosolic superoxide dismutase (Sod1) results in several
air-dependent mutant phenotypes, including methionine
auxotrophy and oxygen sensitivity. Here we report that these two
sod1
Volume 271, Number 46,
Issue of November 15, 1996
pp. 28831-28836
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
Division of Toxicological Sciences,
Department of Environmental Health Sciences, Johns Hopkins University
School of Hygiene and Public Health, Baltimore, Maryland 21205 and the
¶ Department of Biochemistry, State University of New York,
Buffalo, New York 14214
phenotypes were specifically suppressed by elevated
expression of the TKL1 gene, encoding transketolase of the
pentose phosphate pathway. The apparent connection between Sod1 and the
pentose phosphate pathway prompted an investigation of mutants
defective in glucose-6-phosphate dehydrogenase (Zwf1), which catalyzes
the rate-limiting NADPH-producing step of this pathway. We confirmed
that zwf1 mutants are methionine auxotrophs and report
that they also are oxygen-sensitive. We determined that a functional
ZWF1 gene product was required for TKL1 to
suppress sod1, leading us to propose that increased flux
through the oxidative reactions of the pentose phosphate pathway can
rescue sod1 methionine auxotrophy. To better understand
this methionine growth requirement, we examined the sulfur compound
requirements of sod1 and zwf1 mutants,
and noted that these mutants exhibit the same apparent defect in sulfur
assimilation. Our studies suggest that this defect results from the
impaired redox status of aerobically grown sod1 and
zwf1 mutants, implicating Sod1 and the pentose phosphate
pathway as being critical for maintenance of the cellular redox
state.
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