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  • 1
    Electronic Resource
    Electronic Resource
    Hyperosmotic stress response and regulation of cell wall integrity in Saccharomyces cerevisiae share common functional aspects (2001)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 41 (2001), S. 0 
    Details
    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
    URL: http://dx.doi.org/10.1046/j.1365-2958.2001.02549.x
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  • 2
    Electronic Resource
    Electronic Resource
    The control of intracellular glycerol in Saccharomyces cerevisiae influences osmotic stress response and resistance to increased temperature (2000)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 36 (2000), S. 0 
    Details
    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
    URL: http://dx.doi.org/10.1046/j.1365-2958.2000.01955.x
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  • 3
    Electronic Resource
    Electronic Resource
    C-terminal domains of general regulatory factors Abf1p and Rap1p in Saccharomyces cerevisiae display functional similarity (1996)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 19 (1996), S. 0 
    Details
    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
    URL: http://dx.doi.org/10.1046/j.1365-2958.1996.404939.x
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  • 4
    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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  • 5
    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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  • 6
    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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  • 7
    Electronic Resource
    Electronic Resource
    Mutational analysis of the upstream activation site of yeast ribosomal protein genes (1989)
    Springer
    Current genetics 15 (1989), S. 247-251 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00447039
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  • 8
    Electronic Resource
    Electronic Resource
    The cellular level of yeast ribosomal protein L25 is controlled principally by rapid degradation of excess protein (1986)
    Springer
    Current genetics 10 (1986), S. 733-739 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00405095
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  • 9
    Electronic Resource
    Electronic Resource
    The gene for yeast ribosomal protein S31 contains an intron in the leader sequence (1985)
    Springer
    Current genetics 10 (1985), S. 1-5 
    Details
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00418486
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  • 10
    Electronic Resource
    Electronic Resource
    Structural and putative regulatory sequences of the gene encoding ribosomal protein L25 in Candida utilis (1987)
    Springer
    Current genetics 12 (1987), S. 193-198 
    Details
    ISSN: 1432-0983
    Keywords: Candida utilis ; Gene structure ; Ribosomal protein L25
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Using a heterologous probe containing a fragment of the L25-gene from Saccharomyces carlsbergensis we have isolated a DNA-fragment of Candida utilis carrying the gene encoding ribosomal protein L25. This gene is present in a single copy on the C. utilis genome, though as two distinguishable alleles. Both alleles have been isolated and sequenced including their flanking regions. The nucleotide sequence of the amino acid coding region of the C. utilis gene turned out to be highly homologous (83%) to the L25-gene of S. carlsbergensis. At the protein level the degree of homology is about 87%. Codon usage in both organisms appears to be somewhat different. Just like the Saccharomyces gene, the L25 gene in C. utilis appears to be split in its 5th codon, though the identity of this codon has changed. Intron as well as 5′- and 3′-flanking sequences have almost completely diverged, with some notable exceptions. Of the intervening sequences the 5′- and 3′-splice sites as well as the putative lariat branch site are conserved. In the 5′-flanking region, at a distance of about 330 n from the initiation codon, a conserved nucleotide element is present that is very similar to the upstream transcription activation site previously found in front of the ribosomal protein genes in Saccharomyces.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00436878
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