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  • Blackwell Publishing Ltd  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    Osmostress response of the yeast Saccharomyces (1993)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 10 (1993), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Exposure of yeast cells to high osmolarities leads to dehydration, collapse of ion gradients over the plasma membrane and decrease in cell viability. The response of yeast cells to high external osmolarities is designated osmostress response. It is likely that both osmoregulatory and general stress reactions are involved in this so far poorly understood process. Part of the response aims at raising the internal osmotic potential, i.e. the production of osmolytes such as glycerol, and exclusion of toxic solutes. In addition, heat-shock proteins and trehalose are synthesized, probably to protect cellular components and to facilitate repair and recovery. Recent analyses of osmosensitive yeast mutants strongly suggest the involvement of protein kinase-mediated signal-transduction pathways in the maintenance of the osmotic integrity of the cell. This has stimulated interesting hypotheses as to the actual osmosensing mechanism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1993.tb01951.x
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  • 2
    Electronic Resource
    Electronic Resource
    Osmostress-induced changes in yeast gene expression (1992)
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 6 (1992), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: When Saccharomyces cerevisiae cells are exposed to high concentrations of NaCI, they show reduced viability, methionine uptake and protein biosynthesis. Cells can acquire tolerance against a severe salt shock (up to 1.4 M NaCI) by a previous treatment with 0.7 M NaCI, but not by a previous heat shock. Two-dimensional analysis of [3H]-leucine-labelled proteins from salt-shocked cells (0.7 M NaCt) revealed the elevated rate of synthesis of nine proteins, among which were the heat-shock proteins hsp12 and hsp26. Northern analysis using gene-specific probes confirmed the identity of the latter proteins and, in addition, demonstrated the induction of glycerol-3-phos-phate dehydrogenase gene expression. The synthesis of the same set of proteins is induced or enhanced upon exposure of cells to 0.8 M sucrose, although not as dramatically as in an iso-osmolar NaCI concentration (0.7 M).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.1992.tb01392.x
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  • 3
    Electronic Resource
    Electronic Resource
    Nutritional upshift response of ribosomal protein gene transcription in Saccharomyces cerevisiae (1994)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 123 (1994), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Switching Saccharomyces cerevisiae from non-fermentative to fermentative growth by adding glucose to a medium with glycerol as the sole carbon source, leads to a sudden increase in the rate of ribosomal protein gene transcription. By analyzing the nutritional shift response in a variety of yeast mutants and in the presence of different drugs, evidence was obtained that: (i) no de novo protein synthesis is required for this response; (ii) protein kinase A is essential, though independent of intracellular levels of cAMP, whereas protein kinase C is not involved; (iii) proper regulation of sugar phosphorylation is essential; (iv) glycolysis is required for the long term effect of the nutritional upshift; and (v) pathways leading to glucose-induced activation differ from those leading to gene repression, probably already at the level of glucose transport.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1994.tb07213.x
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