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Volume 272, Number 9,
Issue of February 28, 1997
pp. 5544-5554
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Metabolic and Regulatory Changes Associated with Growth of
Saccharomyces cerevisiae in 1.4 M NaCl
EVIDENCE FOR OSMOTIC INDUCTION OF GLYCEROL DISSIMILATION VIA
THE DIHYDROXYACETONE PATHWAY
(Received for publication, July 23, 1996, and in revised form, November 25, 1996)
Joakim
Norbeck
and
Anders
Blomberg
From the Department of General and Marine Microbiology,
Göteborg University, Medicinaregatan 9 C,
413 90 Göteborg, Sweden
The salt-instigated protein expression of
Saccharomyces cerevisiae during growth in either 0.7 or 1.4 M NaCl was studied by two-dimensional polyacrylamide gel
electrophoresis. The 73 protein spots that were identified as more than
3-fold responsive in 1.4 M NaCl were further grouped by
response class (halometric, low-salt, and high-salt regulation).
Roughly 40% of these responsive proteins were found to decrease in
expression, while at higher magnitudes of change (>8-fold) only
induction was recorded. Enolase 1 (Eno1p) was the most increasing
protein by absolute numbers per cell, but not by -fold change, and the
enzymes involved in glycerol synthesis, Gpd1p and Gpp2p, were also
induced to a similar degree as Eno1p. We furthermore present evidence
for salt induction of glycerol dissimilation via dihydroxyacetone and
also identify genes putatively encoding the two enzymes involved;
dihydroxyacetone kinase (DAK1 and DAK2) and
glycerol dehydrogenase (YPR1 and GCY1). The
GPD1, GPP2, GCY1, DAK1,
and ENO1 genes all displayed a halometric increase in the
amount of transcript. This increase was closely linked to the
salt-induced rate of protein synthesis of the corresponding proteins,
indicating mainly transcriptional regulation of expression for these
genes. A consensus element with homology to the URS sequence of the
ENO1 promoter was found in the promoters of the GPD1, GPP2, GCY1, and
DAK1 genes.

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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.
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