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  • 1
    Online Resource
    Online Resource
    Berlin, Heidelberg :Springer Berlin / Heidelberg,
    Keywords: Yeast fungi-Effect of stress on. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (398 pages)
    Edition: 1st ed.
    ISBN: 9783540456117
    Series Statement: Topics in Current Genetics Series ; v.1
    DDC: 571.2/9562
    Language: English
    Note: Intro -- Yeast Stress Responses -- Table of Contents -- List of contributors -- 1 Introduction -- What is stress? -- Studies of stress responses -- Cell proliferation and stress -- Aim of the stress response -- Phases of the stress response -- Sensing and signalling -- Adaptation to stress -- Yeast as a model -- 2The environmental stress response: a common yeast response to diverse environmental stresses -- 2.1 Introduction -- 2.2 The environmental stress response -- 2.3 Responsiveness of ESR gene expression -- 2.4 Transcript levels versus protein synthesis levels -- 2.5 Functions represented by genes repressed in the ESR -- 2.5.1 Ribosome synthesis -- 2.5.2 tRNA synthesis -- 2.5.3 General transcription -- 2.5.4 RNA splicing and export -- 2.5.5 Translation -- 2.6 Functions represented by genes induced in the ESR -- 2.6.1 Carbohydrate metabolism -- 2.6.2 Fatty acid metabolism -- 2.6.3 Respiration -- 2.6.4 Oxidative stress defense -- 2.6.5 Autophagy and vacuolar functions -- 2.6.6 Protein folding and degradation -- 2.6.7 Cytoskeletal reorganization -- 2.6.8 Signaling -- 2.7 Functional themes in the ESR -- 2.7.1 Differential expression of isozymes -- 2.7.2 Coinduction of genes with counterproductive functions -- 2.7.3 Regulation of control steps of metabolic processes -- 2.8 The role of the ESR -- 2.9 Regulation of ESR gene expression -- 2.9.1 Rap1p -- 2.9.2 Chromatin remodeling -- 2.9.3 Regulated mRNA turnover -- 2.9.4 Msn2p and Msn4p -- 2.9.5 Condition-specific transcriptional induction -- 2.9.6 Condition-specific cellular signaling -- 2.9.7 Advantages of the complex regulation of ESR gene expression -- 2.10 Orchestration of cellular responses to stress -- 2.11 Conclusions -- 3 The yeast response to heat shock -- 3.1 Introduction -- 3.2 The heat shock and environmental stress responses. , 3.2.1 Transcriptional regulators of heat shock gene induction -- 3.2.2 Delineation of the Hsf1p and Msn2p/Msn4p heat shock regulons -- 3.2.3 The role of trehalose in thermotolerance -- 3.2.4 Thermal stress phenotypes in yeast -- 3.3 Regulation of the heat shock factor Hsf1p -- 3.3.1 Regulation of Hsf1p transcriptional activation -- 3.3.2 The role of phosphorylation in Hsf1p regulation -- 3.3.3 Genetic and structural insights into DNA binding and regulation -- 3.3.4 Sensing the proteome: regulation by protein chaperones -- 3.3.5 Hsf1p-like proteins in yeast -- 3.3.6 Hsf1p and the cell cycle -- 3.4 New directions in protein chaperone biology -- 3.4.1 Hsp90 chaperone complex subunits in yeast -- 3.4.2 Endogenous yeast Hsp90 substrates -- 3.4.3 Protein chaperones and yeast prion propagation -- 3.5 Stress and aging -- 3.6 Conclusions -- 4 The osmotic stress response of Saccharomyces cerevisiae -- 4.1 Introduction -- 4.2 Structural and morphological effects caused by osmotic stress -- 4.3 Glycerol and glycerol metabolism -- 4.3.1 Glycerol metabolic pathways -- 4.3.2 Glycerol transport -- 4.3.3 Glycerol accumulation under osmotic stress: multiple levels of control -- 4.4 Transport processes affected by osmotic stress -- 4.4.1 MIP channels: aquaporins and glycerol channels -- 4.4.2 Osmolyte uptake systems -- 4.4.3 Ion channels -- 4.5 Perception of and response to osmotic stress: the role of signalling pathways -- 4.5.1 S. cerevisise MAPK pathways -- 4.5.2 The HOG MAPK pathway in Saccharomyces cerevisise -- 4.5.3 Control of gene expression -- 4.5.4 The cell integrity pathway -- 4.5.5 Skn7p: a putative link between osmosensing pathways -- 4.5.6 Additional systems involved in osmotic stress signalling -- 4.5.7 Mechanisms of osmosensing -- 4.6 Metabolic adjustments -- 4.7 Osmotic signalling in other yeasts: the S. pombe Sty1 pathway -- 4.8 Conclusions. , 5 Ion homeostasis in Saccharomyces cerevisiae under NaCl stress -- 5.1 Introduction -- 5.2 Yeast Na+ and K+ relations -- 5.2.1 Growth and intracellular ion levels -- 5.2.2 Why is K but not Na a preferred intracellular cation? -- 5.2.3 Na toxicity -- 5.3 Adaptation to high concentrations of salt: role of ion transporters -- 5.3.1 The plasma membrane H -ATPase -- 5.3.2 K transport systems -- 5.3.3 The Pmr2Ap/Ena1p sodium transporter -- 5.3.4 The Nha1p Na /H antiporter -- 5.3.5 Compartmentalization of Na -- 5.4 Regulation of ion homeostasis -- 5.4.1 Control at transcriptional level: ENA1 -- 5.4.2 Control on protein level -- 5.4.3 Regulation of the Trk1/2p system -- 5.5 Ion transporters and membrane targeting -- 5.5.1 Targeting of P-type ATPases to the plasma membrane -- 5.5.2 Nhx1p is involved in membrane traffic out of the prevacuolar compartment -- 5.6 The genome-wide transcriptional response -- 5.7 Conclusions -- 6 Oxidative stress responses in yeast -- 6.1 Introduction -- 6.2 Effects of oxygen free radicals on biological molecules -- 6.2.1 Some concepts of free radical chemistry -- 6.3 Biological effects of oxygen free radicals in yeast -- 6.3.1 Methods for measuring the cellular toxicity of ROS -- 6.3.2 Cellular effects of ROS in S. cerevisiae -- 6.4 Antioxidant defenses and thiol redox homeostasis -- 6.4.1 Metal containing antioxidants -- 6.4.2 Thiol redox control pathways and peroxidase systems -- 6.5 Adaptive oxidative stress responses -- 6.5.1 S. cerevisiae adaptive responses to oxidative stress -- 6.5.2 The genomic response underlying oxidative stress adapted states -- 6.6 Control of S. cerevisiae oxidative stress responses -- 6.6.1 The Yap1 pathway -- 6.6.2 Skn7 as a stress response coordinator -- 6.6.3 An H2O2-inducible Msn2/4 pathway -- 6.5.4 Other regulators of the oxidative stress response in S. cerevisiae. , 6.7 Control of S. pombe oxidative stress responses -- 6.7.1 The stress-activated MAP kinase pathway -- 6.7.2 Atf1, a bZip transcription factor substrate of Spc1/Sty1 -- 6.7.3 The S. pombe Yap1 homologue Pap1 -- 6.7.4 The response regulator Prr1, a homologue of Skn7 -- 6.7.5 Two two-component phosphorelay systems contribute to the H2O2 response -- 6.8 Regulators of the oxidative stress response in other yeasts -- 6.9 Conclusions -- 7 From feast to famine -- adaptation to nutrient availability in yeast -- 7.1 Introduction -- 7.2 Setting the stage: limitation, starvation, and cell cycle checkpoints -- 7.3 Specific responses to nutrient depletion -- 7.3.1 Carbon Source Signalling -- 7.3.2 Nitrogen Source Signalling -- 7.3.3 Phosphor Limitation and Starvation -- 7.3.4 Sulphur Limitation and Starvation -- 7.4 Common responses to nutrient depletion -- 7.4.1 General Concepts -- 7.4.2 Nutrient signal integration and the control of metabolism and growth -- 7.4.3 The FGM pathway -- an integrator of responses to nutrient availability -- 7.4.4 Nutritional control by targets of rapamycin (Tor) proteins -- 7.4.5 Glycogen and Trehalose metabolism -- 7.4.6 Morphological differentiation as a response to nutrient limitation -- 7.5 Conclusions -- Index.
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  • 2
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The osmosensitive phenotype of the hog1 strain is suppressed at elevated temperature. Here, we show that the same holds true for the other commonly used HOG pathway mutant strains pbs2 and sho1ssk2ssk22, but not for ste11ssk2ssk22. Instead, the ste11ssk2ssk2 strain displayed a hyperosmosensitive phenotype at 37°C. This phenotype is suppressed by overexpression of LRE1, HLR1 and WSC3, all genes known to influence cell wall composition. The suppression of the temperature-induced hyperosmosensitivity by these genes prompted us to investigate the role of STE11 and other HOG pathway components in cellular integrity and, indeed, we were able show that HOG pathway mutants display sensitivity to cell wall-degrading enzymes. LRE1 and HLR1 were also shown to suppress the cell wall phenotypes associated with the HOG pathway mutants. In addition, the isolated multicopy suppressor genes suppress temperature-induced cell lysis phenotypes of PKC pathway mutants that could be an indication for shared targets of the PKC pathway and high-osmolarity response routes.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Glycerol has been demonstrated to serve as the major osmolyte of Saccharomyces cerevisiae. Consistently, mutant strains gpd1gpd2 and gpp1gpp2, which are devoid of the main glycerol biosynthesis pathway, have been shown to be osmosensitive. In addition, the primary hyperosmotic stress response is affected in these strains. Hog1p phosphorylation turned out to be prolonged and osmostress-induced gene expression is delayed compared with the kinetics observed in wild-type cells. A hog1 deletion strain was previously found to contain lower internal glycerol and therefore displays an osmosensitive phenotype. Here, we show that the osmosensitivity of hog1 is suppressed by growth at 37°C. We reasoned that this temperature-remedial osmoresistance might be caused by a higher intracellular glycerol level at the elevated temperature. This hypothesis was confirmed by measurement of the glycerol concentration, which was shown to be similar for wild type and hog1 cells only at elevated growth temperatures. In agreement with this finding, hog1 cells containing an fps1 allele, encoding a constitutively open glycerol channel, have lost their temperature-remedial osmoresistance. Furthermore, gpd1gpd2 and gpp1gpp2 strains were found to be temperature sensitive. The growth defect of these strains could be suppressed by adding external glycerol. In conclusion, the ability to control glycerol levels influences proper osmostress-induced signalling and the cellular potential to grow at elevated temperatures. These data point to an important, as yet unidentified, role of glycerol in cellular functioning.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Abf1p and Rap1p are global regulatory factors which play an essential role in the transcription activation of yeast ribosomal protein genes. This functional link prompted us to investigate whether these factors may be functionally interchangeable. We focused on the indispensable C-terminal portions of both factors and performed mutual domain swaps. The functional capacity of the resulting hybrid proteins was subsequently examined using yeast strains conditionally expressing either the ABF1 or the RAP1 gene. Both the Abf1p–Rap1p and the Rap1p–Abf1p fusion proteins were found to be able to complement the growth defect of the respective strains. Furthermore, Abf1p and Rap1p are both able to promote transcription of a reporter gene through a combination of the respective binding site and a T-rich promoter element. These data strongly suggest that the C-terminal domains of Abf1p and Rap1p have, at least partially, identical functions. Finally, a deletion analysis of the so far largely uncharacterized C-terminal domain of Abf1p was performed, which revealed that two regions of 50 amino acids can perform all essential Abf1p functions.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 10 (1993), S. 0 
    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
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Molecular microbiology 6 (1992), S. 0 
    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
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 123 (1994), S. 0 
    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
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  • 8
    ISSN: 1432-0983
    Keywords: Yeast ; Ribosomal protein gene ; Transcription activation ; Mutation ; Methylation interference
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Most ribosomal protein (rp-)genes in yeast are preceded by conserved sequence motifs that act as upstream transcription-activating sites (RPG box). These sequence elements have previously been shown to represent specific binding sites for a protein factor, TUF. Comparison of the various nucleotide elements identified so far indicates a remarkably high degree of variation in the respective sequences. On the other hand, a methylation interference study performed with one RPG box revealed close contact points with the TUF protein along the entire sequence. To investigate the sequence requirements of the RPG box, we inserted synthetic oligonucleotides that differed from the general consensus sequence ACACCCATACATTT at single positions into a deletion mutant of the L25 promoter that lacked its natural RPG elements. Transcription activity was estimated by Northern analyses of the cellular level of L25-galK hybrid transcripts. The results show that in the 3′ part of this sequence element single substitutions are allowed at all positions, in the 5′ part, however, the nucleotide requirements appear to be more stringent. In particular, the invariant C at position 5 of the consensus sequence is absolutely necessary for its enhancer function.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1432-0983
    Keywords: Yeast ; Ribosome synthesis ; Regulation ; Ribosomal protein turnover
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary When the gene dosage for the primary rRNA-binding ribosomal protein L25 in yeast cells was raised about 50-fold, the level of mature L25 transcripts was found to increase almost proportionally. The plasmid-derived L25 transcripts were structurally indistinguishable from their genomic counterparts, freely entered polysomes in vivo and were fully translatable in a heterologous in vitro system. Nevertheless, pulse-labelling for periods varying from 3–20 min did not reveal a significant elevation of the intracellular level of L25 protein. When pulse-times were decreased to 10–45 s, however, we did detect a substantial over production of L25. We conclude that, despite the strong RNA-binding capacity of the protein, accumulation of L25 is not controlled by an autogenous (pre-)mRNA-targeted mechanism similar to that operating in bacteria, but rather by extremely rapid degradation of excess protein produced.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1432-0983
    Keywords: Posttranslational processing ; Ribosomal protein gene ; Transcript mapping ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Analysis of the primary structure of the gene for yeast ribosomal protein S31 revealed two unusual features. First, an intron of 312 nucleotides is located within the 5′-untranslated region. Second, the coding sequence for the known amino-terminal peptide of the protein starts 13 codons downstream of the ATG initiation codon, suggesting that S31 is synthesized as a precursor which undergoes post-translational processing to the mature protein. Primer extension analysis showed that transcription of the S31 gene starts at multiple sites. The 5′-flanking region of the gene contains several, previously described, conserved sequence elements that may play a role in the coordinate expression of yeast ribosomal protein genes.
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