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(Received for publication, July 23, 1996, and in revised form, November 25, 1996)
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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