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  • 1
    Electronic Resource
    Electronic Resource
    Differential synthesis of glyceraldehyde-3-phosphate dehydrogenase polypeptides in stressed yeast cells (1995)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 125 (1995), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Three unlinked genes, TDH1, TDH2 and TDH3, encode the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (triose-phosphate dehydrogenase; TDK) in the yeast Saccharomyces cerevisiae. We demonstrate that the synthesis of the three encoded TDK polypeptides (TDHa, TDHb and TDHc, respectively) is not co-ordinately regulated and that TDHa is only synthesised as cells enter stationary phase, due to glucose starvation, or in heat-shocked cells. Furthermore, the synthesis of TDHb, but not TDHc, is strongly repressed by a heat shock. Hence, the TDHa enzyme may play a cellular role, distinct from glycolysis, that is required by stressed cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1995.tb07348.x
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  • 2
    Electronic Resource
    Electronic Resource
    Role of the Myb-like protein Bas1p in Saccharomyces cerevisiae: a proteome analysis (1998)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 30 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The effect of extracellular adenine and the role of the transcriptional activator Bas1p on expression of the yeast genome was assessed by two-dimensional (2D) analysis of the yeast proteome. These data combined with LacZ fusions and northern blot analysis allow us to show that synthesis of enzymes for all 10 steps involved in purine de novo synthesis is repressed in the presence of adenine and requires BAS1 and BAS2 for optimal expression. We also show that expression of ADE12 and ADE13, the two genes required for synthesis of AMP from inosine 5′monophosphate (IMP), is co-regulated with the de novo pathway genes. The same combined approach, used to study histidine biosynthesis gene expression, showed that HIS1 and HIS4 expression is co-regulated with purine biosynthesis genes whereas HIS2, HIS3, HIS5 and HIS6 expression is not. This work, together with previously published data, gives the first comprehensive overview of the regulation of purine and histidine pathways in a eukaryotic organism. Finally, the expression of two pyrimidine biosynthesis genes URA1 and URA3 was found to be severely affected by bas1 and bas2 mutations in the absence of adenine, establishing a regulatory link between the two nucleotide biosynthesis pathways.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.01087.x
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  • 3
    Electronic Resource
    Electronic Resource
    Isolation and sequence of HSP30, a yeast heat-shock gene coding for a hydrophobic membrane protein (1993)
    Springer
    Current genetics 23 (1993), S. 435-442 
    Details
    ISSN: 1432-0983
    Keywords: Heat shock ; Recombinant DNA ; Membrane protein ; Nutritional limitation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Using differential hybridization, a gene preferentially expressed during entry into stationary phase has been isolated. Subsequent analysis indicated that this gene corresponds to a heat-shock gene. The nucleotide sequence has been determined. It revealed a 332 aminoacid protein. No similarities to any previously known protein have been noted. The protein is very hydrophobic and is predicted to have a membraneous localisation. In agreement with this hypothesis, the analysis of membrane proteins from stationary-phase cells showed that a strain carrying this gene on a multicopy vector overproduces a protein of 30 kDa. This protein was recognized by antibodies directed against the N-terminal portion of the gene product. Considering its induction in response to heat shock and the apparent molecular weight of its product, this gene was designated HSP30.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00312631
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  • 4
    Electronic Resource
    Electronic Resource
    Protoplasmic incompatibility and the genetic control of stable messenger RNAs (1983)
    Springer
    Biochemical genetics 21 (1983), S. 287-297 
    Details
    ISSN: 1573-4927
    Keywords: stable messenger RNAs ; protoplasmic incompatibility ; Podospora anserina
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract In Podospora anserina, protoplasmic incompatibility due to the combination of nonallelic genes is suppressed by the addition of a recessive mutation in the modA gene to a dominant mutation in the modB gene. The effect of the modA and modB mutations on several features of protoplasmic incompatibility was investigated. Results show that the modA mutation suppresses two of them: the shutoff of RNA synthesis and the inhibition of synthesis of normal proteins. The suppression of a third feature of protoplasmic incompatibility, i.e., the synthesis of specific proteins, involves both the modA and the modB mutations. Employing the dihydrostreptomycin sensitivity of the modA gene product, it is shown that the modA gene controls the synthesis of one of these proteins (laccase III) at a posttranscriptional level. Concerning the modB gene, its effect was studied by means of a thermosensitive recessive mutation in this gene. It is demonstrated that the presence of this mutation results in the occurrence, in the cell extract, of enzyme activities (laccase III and its associated activities) and polypeptides specific to protoplasmic incompatibility. Furthermore, it could be deduced that the modB gene operates on these syntheses at a posttranscriptional level.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00499139
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  • 5
    Electronic Resource
    Electronic Resource
    Protoplasmic incompatibility and female organ formation in Podospora anserina: Properties of mutations abolishing both processes (1974)
    Springer
    Molecular genetics and genomics 135 (1974), S. 163-174 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A genetic block, effective only with the addition of mutations in two genes, suppresses both the incompatibility process in strain confrontation (“barrage”) and the formation of female organs. Investigations on this block lead us to propose that it operates at the ribosomal level and prevents the translation of the messenger of a proteolytic enzyme, a postulated early protein in protoperithecia differenciation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00264783
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  • 6
    Electronic Resource
    Electronic Resource
    Intracellular and extracellular phenoloxidases in the fungus Podospora anserina: Effect of a constitutive mutation in a gene involved in their posttranscriptional control (1977)
    Springer
    Molecular genetics and genomics 157 (1977), S. 53-59 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Three phenoloxidases- and in particular phenoloxidase B, an enzyme found in cell extracts only in the cases of protoplasmic incompatibility and cell lysis where it occurs in association with a protease — were investigated in a wild type strain. Phenoloxidase B was present only in the culture filtrates, while the other two phenoloxidases were found in cell extracts and in the culture medium. Addition of casaminoacids and ammonium acetate to the culture medium produced opposite effects: under the first conditions, phenoloxidase B increased in being present only in the culture filtrates and in the second medium, like a second phenoloxidase (activity C), phenoloxidase B completely disappeared from the culture filtrates. A recessive mutation was isolated in a gene modB that resulted in the production of phenoloxidases B and C in higher amounts. The temperature dependence of the mutation modB allowed us to show that the formation of the phenoloxidases was 5 Fluorouracilresistant and cycloheximide sensitive, suggesting that constitutivity for these enzymes resulted from a derepression in their posttranscriptional control. Because of this derepression, phenoloxidase B not only increased in the culture medium (30x), but was found in cell extracts in association with a protease whose presence is suspected to produce a premature disintegration of the mycelium. The results are discussed from the point of view of the processes capable of regulating the production of exoenzymes and in relationship with the phenomenon of cell death normally affecting mycelia during ageing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268687
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  • 7
    Electronic Resource
    Electronic Resource
    Two-dimensional gel analysis of yeast proteins: Application to the study of changes in the levels of major polypeptides of Saccharomyces cerevisiae depending on the fermentable or nonfermentable nature of the carbon source (1988)
    Weinheim : Wiley-Blackwell
    Electrophoresis 9 (1988), S. 774-780 
    Details
    ISSN: 0173-0835
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Taking advantage of the recent identification of polypeptides of the carbor meta. bolism machinery on the yeast protein map [1], we applied two-dimensional gel electrophoresis to a study of changes in protein composition of Saccharomyces cerevisiae depending on the fermentable or nonfermentable nature of the carbon source. The levels of the 250 most abundant polypeptides were compared. Thirty-three were found to display markedly increased levels during growth on nonfermenable carbon sources. These 33 polypeptides include 11 mitochondrial polypeptides and polypeptides corresponding to alcohol dehydrogenase II, acetyl-CoA synthetase, phosphoenol pyruvate kinase and hexokinase PI. Sixteen other polypeptides, in contrast, reached their higher levels during growth on fermentable corbon sources. Among these were identified the monomeric subunits of 6 giycoytic enzymes. Collectively the 33 polypeptides of the first class comprised over 30% of the total soluble proteins of cells grown on nonfermentable carbon source and 3 % during growth on fermentable carbon source. The protein fraction of the 16 polypeptides of the second ass corresponded to 10 % and 38 %, respectively. Together these results show that two-dimensional gel electrophoresis, when coupled with the identification of polypeptides of the carbon metabolism apparatus, provides a valuable tool for approaching questions concerning carbon metabolism in S. cerevisiae.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150091113
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  • 8
    Electronic Resource
    Electronic Resource
    Two-dimensional gel protein database of Saccharomyces cerevisiae (1996)
    Weinheim : Wiley-Blackwell
    Electrophoresis 17 (1996), S. 1683-1699 
    Details
    ISSN: 0173-0835
    Keywords: Yeast ; Saccharomyces cerevisiae ; Two-dimensional polyacrylamide gel electrophoresis ; Protein database ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: With the systematic sequencing of the yeast genome, yeast biology has entered a new era where novel challenges have to be faced. One challenge is the identification of the function of the several hundred novel genes discovered by genome sequencing. Another is to understand how all yeast genes act in concert to ensure and maintain cell organization. Two-dimensional (2-D) gel electrophoresis is the technique of choice to take up these challenges because it provides the opportunity of obtaining an overall view of genome expression. In prospect of these studies we have undertaken the construction of a yeast 2-D gel protein database that contains information on polypeptides of the yeast protein map. In this paper we report the information presently contained in this database. The reported information includes the identification of 250 protein spots and the characterization of polypeptides corresponding to N-terminal acetylated proteins, mitochondrial proteins, glucose-repressed proteins, heat shock induced proteins and proteins encoded by intron-containing genes. In all, 600 spots are annotated. These data can be accessed on the Yeast Protein Map server through the World Wide Web network.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/elps.1150171106
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  • 9
    Electronic Resource
    Electronic Resource
    Induction of a heat-shock-type response in Saccharomyces cerevisiae following glucose limitation (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 7 (1991), S. 367-378 
    Details
    ISSN: 0749-503X
    Keywords: S. cerevisiae ; heat-shock proteins ; starvation ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The protein pattern of yeast cells which have arrested proliferation in response to glucose exhaustion is drastically different from that of exponentially growing cells (Boucherie, 1985). In this study, we used two-dimensional gel electrophoresis to characterize the protein events responsible for these alterations. We found that the induction of heat-shock proteins is one of the major events responsible for these changes. This induction accounts for the synthesis of 18 of the 35 novel polypeptides observed in glucose-limited cells. It was shown to occur in combination with two other protein events: the derepression of carbon catabolite repressed proteins, which accounts for the synthesis of the other novel polypeptides, and an arrest of the synthesis of almost all the proteins present in exponentially growing cells.The time course of each of these events was determined by carrying out a detailed analysis of the pattern of proteins synthesized at vaious stages of a culture exhausting its glucose supply, and by the measurement of the rate of synthesis of individual polypeptides. The results showed in particular that the synthesis of most of the heat-shock proteins synthesized in glucose-limited cells was induced closely before glucose exhaustion, and that this synthesis was transient, climaxing by the time glucose was exhausted. Under the culture condition investigated, the entry into stationary phase associated with glucose limitation began several hours before glucose exhaustion. It was thus concluded that the observed induction of heat-shock proteins is directly related to the nutritional limitation and is independent from the arrest of cell proliferation.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320070407
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  • 10
    Electronic Resource
    Electronic Resource
    Identification of polypeptides of the carbon metabolism machinery on the two-dimensional protein map of Saccharomyces cerevisiae. Location of 23 additional polypeptides (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 3 (1987), S. 11-21 
    Details
    ISSN: 0749-503X
    Keywords: Yeast protein map ; carbon metabolism machinery ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Using a modification of the basic two-dimensional polyacrylamide gel electrophoresis technique, we have undertaken a systematic identification of the polypeptides of the protein map of Saccharomyces cerevisiae corresponding to components of the carbon metabolism machinery. To the previous location of nine glycolytic enzyme polypeptides on the yeast protein map we add the location of 23 polypeptides. Ten of them were identified as corresponding to cytoplasmic enzymes of the carbon metabolism machinery and 13 were characterized as mitochondrial proteins. The criteria used to establish the identification of these polypeptides spots include migration with purified proteins, immunodetection, overproduction by plasmid-carrying strains and physiological behaviour.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320030104
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