Catabolite control of the elevation of PGK mRNA levels by heat shock in <i>Saccharomyces cerevisiae</i>

Piper, Peter W.; Curran, Brendan; Davies, Mark W.; Hirst, K.; Lockheart, Alan; Seward, Kevin

doi:10.1111/j.1365-2958.1988.tb00039.x

Cited by 25 publications

(16 citation statements)

References 25 publications

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“…The absorbance at 600 nm was monitored for each culture, and cells were harvested for analysis during the exponential growth phase (A6., 0.6). The doubling time of the lactate culture (275 min) was threefold greater than that for the glucose-grown culture (90 min), which compares favorably with results of previous studies (51).…”

Section: Resultssupporting

confidence: 81%

Yeast glycolytic mRNAs are differentially regulated.

et al. 1991

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The regulation of glycolytic genes in response to carbon source in the yeast Saccharomyces cerevisiae has been studied. When the relative levels of each glycolytic mRNA were compared during exponential growth on glucose or lactate, the various glycolytic mRNAs were found to be induced to differing extents by glucose. No significant differences in the stabilities of the PFK2, PGKI, PYKI, or PDCI mRNAs during growth on glucose or lactate were observed. PYK::lacZ and PGK::lacZ fusions were integrated independently into the yeast genome at the ura3 locus. The manner in which these fusions were differentially regulated in response to carbon source was similar to that of their respective wild-type loci. Therefore, the regulation of glycolytic mRNA levels is mediated at the transcriptional level. When the mRNAs are ordered with respect to the glycolytic pathway, two peaks of maximal induction are observed at phosphofructokinase and pyruvate kinase. These enzymes (i) catalyze the two essentially irreversible steps on the pathway, (ii) are the two glycolytic enzymes that are circumvented during gluconeogenesis and hence are specific to glycolysis, and (iii) are encoded by mRNAs that we have shown previously to be coregulated at the translational level in S. cerevisiae (P. A. Moore, A. J. Bettany, and A. J. P. Brown, NATO ASI Ser. Ser. H Cell Biol. 49:421-432, 1990). This differential regulation of glycolytic mRNA levels might therefore have a significant influence upon glycolytic flux in S. cerevisiae.The glycolytic pathway plays a fundamental role in the provision of metabolic energy and intermediates during fermentative growth in the yeast Saccharomyces cerevisiae. Under these conditions, the glycolytic genes are among the most efficiently expressed genes in this organism, the glycolytic enzymes comprising over 30% of soluble cell protein (for reviews, see references 20 and 70). Most yeast glycolytic genes have been isolated and sequenced (2, 4, 11, 21, 23, 25, 27, 29-31, 40, 59, 62, 63, 68, 69). The high-level expression of yeast glycolytic genes is dependent upon complex interactions between a number of cis-acting promoter elements and trans-acting transcription factors which include the RAP1, ABF1, GCR1, and GAL11 proteins (3,8,10,12,13,15,41,48,55,60,61).It is not clear whether the expression of all glycolytic genes is induced when yeast cultures are transferred from nonfermentative to fermentative carbon sources. Maitra and Lobo (37) observed 3-to 100-fold increases in the levels of glycolytic enzymes following the addition of glucose to yeast cultures growing on acetate. This work was performed on a hybrid yeast strain generated by a cross between Saccharomyces fragilis and Saccharomyces dobzhanskii (37). Some more recent studies appear to confirm this observation for S. cerevisiae. For example, analyses of the enolase (EN02), phosphoglygerate kinase (PGKJ), pyruvate kinase (PYKI), pyruvate decarboxylase (PDCI), and alcohol dehydrogenase (ADHI) mRNAs have suggested that their levels are regulated in response to ...

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Section: Resultssupporting

confidence: 81%

Yeast glycolytic mRNAs are differentially regulated.

et al. 1991

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“…Enolase, along with severa1 other glycolytic enzymes, such as phosphoglycerate kinase and glyceraldehyde 3-phosphate dehydrogenase, has been reported to have heat-shock-responsive expression patterns in yeast (Iida and Yahara, 1985;Piper et al, 1988). In tomato root and leaf tissues, however, heat shock resulted in a transient decline in enolase mRNA accumulation, followed by a return to normal levels (Van Der Straeten et al, 1991).…”

Section: Discussionmentioning

confidence: 98%

Posttranscriptional and Posttranslational Control of Enolase Expression in the Facultative Crassulacean Acid Metabolism Plant Mesembryanthemum crystallinum L

1995

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“…The regulation of PGK1 has earlier been shown to be under heat shock control (35). Even the synthesis of Eno1p is enhanced during heat treatment, and it was the first heat-responding protein to be identified in yeast cells (23).…”

Section: Discussionmentioning

confidence: 99%

Global changes in protein synthesis during adaptation of the yeast Saccharomyces cerevisiae to 0.7 M NaCl

Blomberg

1995

J Bacteriol

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Exponentially growing Saccharomyces cerevisiae was challenged to increased salinity by transfer to 0.7 M NaCl medium, and changes in protein synthesis were examined during the 1st h of adaptation by use of two-dimensional gel electrophoresis coupled to computerized quantification. An impressive number of proteins displayed changes in the relative rate of synthesis, with most differences from nonstressed cells being found at between 20 and 40 min. During this period, 18 proteins exhibited more than eightfold increases in their rates of synthesis and were classified as highly NaCl responsive. Only two proteins were repressed to the same level. Most of these highly NaCl-responsive proteins seemed to constitute gene products not earlier reported to respond to dehydration. Applying a selection criterion to subsequent samples of a twofold change in the relative rate of synthesis, 14 different regulatory patterns were discerned. Most identified glycolytic enzymes exhibited a delayed response, and their rates of synthesis did not change until the middle phase of adaptation, with only a minor decrease in the rate of production. A slight salt-stimulated response was observed for some members of the HSP70 gene family. Overall, the data presented indicate complex intracellular signalling as well as involvement of diverse regulatory mechanisms during the period of adaptation to NaCl.

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Catabolite control of the elevation of PGK mRNA levels by heat shock in Saccharomyces cerevisiae

Cited by 25 publications

References 25 publications

Yeast glycolytic mRNAs are differentially regulated.

Yeast glycolytic mRNAs are differentially regulated.

Posttranscriptional and Posttranslational Control of Enolase Expression in the Facultative Crassulacean Acid Metabolism Plant Mesembryanthemum crystallinum L

Global changes in protein synthesis during adaptation of the yeast Saccharomyces cerevisiae to 0.7 M NaCl

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