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  • 1
    Electronic Resource
    Electronic Resource
    A two-reporter gene system for the analysis of bi-directional transcription from the divergent MAL6T-MAL6S promoter in Saccharomyces cerevisiae (1995)
    Springer
    Current genetics 28 (1995), S. 441-446 
    Details
    ISSN: 1432-0983
    Keywords: Divergent promoter ; Maltose ; Transcriptional reporter ; MEL1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Many sets of genes in Saccharomyces cerevisiae are divergently transcribed, but at present there are no vectors generally available for the simultaneous analysis of divergent transcription from these promoters. In the present study MEL1 and lacZ were used to construct a vector capable of measuring the divergent expression initiated by the MAL6T-MAL6S bi-directional promoter. Our observations demonstrate that the expression of both reporter genes was regulated in a similar fashion to the native MAL6T and MAL6S genes, and that induction was dependent upon the presence of a functional MALR activator gene. The results confirmed that the MAL6T-MAL6S promoter was co-ordinately regulated, repressed by glucose, induced by maltose, and that basal expression was more active in the MAL6S direction than in the MAL6T direction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00310813
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  • 2
    Electronic Resource
    Electronic Resource
    Glutathione is an essential metabolite required for resistance to oxidative stress in the yeastSaccharomyces cerevisiae (1996)
    Springer
    Current genetics 29 (1996), S. 511-515 
    Details
    ISSN: 1432-0983
    Keywords: Oxidative stress ; Glutathione ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Glutathione (GSH) is an abundant cellular thiol which has been implicated in numerous cellular processes and in protection against stress caused by xenobiotics, carcinogens and radiation. Our experiments address the requirement for GSH in yeast, and its role in protection against oxidative stress. Mutants which are unable to synthesis GSH due to a gene disruption inGSH 1, encoding the enzyme for the first step in the biosynthesis of GSH, require exogenous GSH for growth under non-stress conditions. Growth can also be restored with reducing agents containing a sulphydryl group, including dithiothreitol, β-mercaptoethanol and cysteine, indicating that GSH is essential only as a reductant during normal cellular processes. In addition, theGSH 1-disruption strain is sensitive to oxidative stress caused by H2O2 and tert-butyl hydroperoxide. The requirement for GSH in protection against oxidative stress is analogous to that in higher eukaryotes, but unlike the situation in bacteria where it is dispensable for growth during both normal and oxidative stress conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02426954
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  • 3
    Electronic Resource
    Electronic Resource
    Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae (1996)
    Springer
    Current genetics 29 (1996), S. 511-515 
    Details
    ISSN: 1432-0983
    Keywords: Key words  Oxidative stress ; Glutathione ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract   Glutathione (GSH) is an abundant cellular thiol which has been implicated in numerous cellular processes and in protection against stress caused by xenobiotics, carcinogens and radiation. Our experiments address the requirement for GSH in yeast, and its role in protection against oxidative stress. Mutants which are unable to synthesis GSH due to a gene disruption in GSH 1, encoding the enzyme for the first step in the biosynthesis of GSH, require exogenous GSH for growth under non-stress conditions. Growth can also be restored with reducing agents containing a sulphydryl group, including dithiothreitol, β-mercaptoethanol and cysteine, indicating that GSH is essential only as a reductant during normal cellular processes. In addition, the GSH 1-disruption strain is sensitive to oxidative stress caused by H2O2 and tert-butyl hydroperoxide. The requirement for GSH in protection against oxidative stress is analogous to that in higher eukaryotes, but unlike the situation in bacteria where it is dispensable for growth during both normal and oxidative stress conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050079
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  • 4
    Electronic Resource
    Electronic Resource
    Leu343Phe substitution in the Malx3 protein of Saccharomyces cerevisiae increases the constitutivity and glucose insensitivity of MAL gene expression (1999)
    Springer
    Current genetics 35 (1999), S. 491-498 
    Details
    ISSN: 1432-0983
    Keywords: Key words Maltose ; Maltase ; Maltose transcriptional activator ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract To utilise maltose as a carbon source Saccharomyces cerevisiae needs one or more functional MAL loci that contain the MALx1 gene encoding maltose permease, MALx2 encoding maltase, and MALx3 encoding a transcriptional activator. Maltose causes a rapid MALx3-dependent induction of MAL gene transcription, and glucose represses this activation via Mig1p. A MALx3 gene conveying high MAL gene expression in the absence of maltose in a malx3 laboratory mutant strain has been isolated from baker's yeast. The construction of hybrid genes between the isolated gene and a highly regulated MALx3 gene showed that constitutivity was the result of multiple amino-acid alterations throughout the structural gene. The combined effect of these amino-acid alterations was shown to be stronger than the sum of their individual effects on constitutivity. Analysis in glucose-repressed conditions confirmed that increased MALx3 transcript levels increased the glucose insensitivity of MAL gene expression but did not affect constitutivity. Analysis of four mutations between aa 343 and 375, lying within a proposed negative regulatory domain, showed that the single mutation of Leu343Phe increased the glucose insensitivity of MAL gene expression by 30-fold. These results demonstrate that not only Mig1p modulation of MALx3 expression, but also the MALx3 protein structure, is involved in the glucose-insensitive expression of the MAL genes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050444
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  • 5
    Electronic Resource
    Electronic Resource
    Characterisation of carbon dioxide-inducible genes of the marine bacterium, pseudomonas sp. S91 (1996)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 140 (1996), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Characterisation of two genes in Pseudomonas sp. S91 that are responsive to carbon dioxide is reported. These were identified by random transposon mutagenesis leading to fusion of the Escherichia coli lacZ reporter gene to the genes of interest. Expression of the genes' promoters was quantified by measuring the reporter gene product, β-galactosidase. β-Galactosidase synthesis was induced when cells were exposed to 10% CO2 on solid media or during growth in aqueous phase when the culture density was greater than 1 at 610 nm, in either rich or minimal media. Induction of β-galactosidase synthesis was not due to: increased alkalinity, onset of stationary phase, build up of soluble metabolites in the culture supernatant, or cell density-dependent signalling. The CO2-inducible gene fusions were not induced by other environmental conditions that are known to stimulate global regulators of environmental gene expression. Benzole acid (2 mM) induced β-galactosidase synthesis in one of the mutants indicating the CO2 response may involve the intracellular CO2 partial pressure/bicarbonate ion concentration/pH equilibrium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1996.tb08311.x
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  • 6
    Electronic Resource
    Electronic Resource
    Stationary-phase induction of GLR1 expression is mediated by the yAP-1 transcriptional regulatory protein in the yeast Saccharomyces cerevisiae (1996)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 22 (1996), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Glutathione (GSH) is an abundant low-molecular-mass thiol which has been implicated in numerous cellular processes including protection against cytotoxic agents such as xenobiotics, carcinogens and free radicals. Utilization of GSH results in its conversion to the oxidized form (GSSG), and it is recycled to GSH by the action of glutathione reductase (GLR) using the reducing power of NADPH. We show that GLR activity is increased by three- to fourfold during stationary-phase growth compared to exponential phase growth, and that a yeast strain deleted for GLR1, encoding glutathione reductase, shows an elevated sensitivity to H2O2 challenge during stationary phase. These data indicate an increased requirement for GSH as the cell arrests growth and enters stationary phase. The stationary-phase increase in GLR activity is entirely dependent upon the action of the yAP-1 transcriptional regulatory protein, previously implicated in regulating GLR activity in response to oxidative stress. Thus, both oxidant- and growth phase-mediated control of GLR1 expression are regulated by the same transcriptional control mechanism. In addition, strains lacking GLR or yAP-1 do not accumulate GSSG during stationary-phase growth, indicating that the cell possesses alternative means of preventing an accumulation of GSSG during stationary phase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1996.d01-1727.x
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  • 7
    Electronic Resource
    Electronic Resource
    Specific induction by glycine of the gene for the P-subunit of glycine decarboxylase from Saccharomyces cerevisiae (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: The glycine decarboxylase complex (GDC) is composed of four subunits referred to as H-, L-, P-, and T-proteins. The Saccharomyces cerevisiaeGCV2 gene, encoding the P-protein has been cloned by complementation of the gsd2 mutation which prevents cells converting glycine to serine or using glycine as the sole nitrogen source. The gene, located on the right arm of chromosome XIII adjacent to TPS1, encodes a product with a Mr of 114 385. Expression of GCV2 was induced by the addition of more than 200 μM glycine in the medium, and a maximal sixfold induction occurred above 1 mM. This response was specific to glycine and was not observed for any other amino acid. Under the same conditions, the intracellular level of glycine increased up to 30-fold. The levels of P- and L-protein transcripts and GDC activity were also elevated in cells grown in the presence of glycine. Deletion analysis of the GCV2 promoter delimited the control region which contains putative regulatory sites for GCN4 and GLN3 transcription factors.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1996.419947.x
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  • 8
    Electronic Resource
    Electronic Resource
    Regulation of the yeast SPS19 gene encoding peroxisomal 2,4-dienoyl-CoA reductase by the transcription factors Pip2p and Oaf1p: β-oxidation is dispensable for Saccharomyces cerevisiae sporulation in acetate medium (1997)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 26 (1997), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The yeast SPS19 gene encoding the peroxisomally targeted 2,4-dienoyl-CoA reductase shares its promoter region (291 bp) with the sporulation-specific gene SPS18. SPS19 is induced during sporulation in diploids but to a lesser extent than SPS18; under oleate induction conditions, SPS19, but not SPS18, is transcribed via an oleate response element (ORE) independently of ploidy or sporulation. The SPS19 ORE is the binding target of the Pip2p and Oaf1p transcription factors, and an SPS19–lacZ reporter gene, which is highly expressed in oleate-induced cells, is not activated in haploids devoid of either protein. We examined the expression of CYC1–lacZ reporter constructs carrying the SPS19 and CTA1 OREs in diploids propagated under sporulation conditions and have shown that OREs are not sufficient for heterologous expression during yeast development. In addition, diploids deleted at either PIP2 or OAF1 demonstrated abundant ascosporogenesis, indicating that these genes are not essential for sporulation. A Δpex6 strain lacking peroxisomal structures and one devoid of fatty acyl-CoA oxidase (Δpox1), the first step in fungal β-oxidation, were both proficient for sporulation and, hence, β-oxidation and the peroxisomal compartment containing it are dispensable for meiotic development.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1997.5931969.x
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  • 9
    Electronic Resource
    Electronic Resource
    Nitrosoguanidine mutagenesis during nuclear and mitochondrial gene replication (1974)
    [s.l.] : Nature Publishing Group
    Nature 250 (1974), S. 709-712 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The timing of individual nuclear gene replication during S phase in an eukaryote can now be studied by nitrosoguanidine mutagenesis. Using this technique, results also suggested that mitochondrial DNA replication is synchronous and a late event in the cell ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/250709a0
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  • 10
    Electronic Resource
    Electronic Resource
    Glutathione regulates the expression of γ-glutamylcysteine synthetase via the Met4 transcription factor (2002)
    Oxford, UK : Blackwell Science, Ltd
    Molecular microbiology 46 (2002), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Our previous studies have shown that glutathione is an essential metabolite in the yeast Saccharomyces cerevisiae because a mutant deleted for GSH1, encoding the first enzyme in γ-l-glutamyl-l-cysteinylglycine (GSH) biosynthesis, cannot grow in its absence. In contrast, strains deleted for GSH2, encoding the second step in GSH synthesis, grow poorly as the dipeptide intermediate, γ-glutamylcysteine, can partially substitute for GSH. In this present study, we identify two high copy suppressors that rescue the poor growth of the gsh2 mutant in the absence of GSH. The first contains GSH1, indicating that γ-glutamylcysteine can functionally replace GSH if it is present in sufficiently high quantities. The second contains CDC34, encoding a ubiquitin conjugating enzyme, indicating a link between the ubiquitin and GSH stress protective systems. We show that CDC34 rescues the growth of the gsh2 mutant by inducing the Met4-dependent expression of GSH1 and elevating the cellular levels of γ-glutamylcysteine. Furthermore, this mechanism normally operates to regulate GSH biosynthesis in the cell, as GSH1 promoter activity is induced in a Met4-dependent manner in a gsh1 mutant which is devoid of GSH, and the addition of exogenous GSH represses GSH1 expression. Analysis of a cis2 mutant, which cannot breakdown GSH, confirmed that GSH and not a metabolic product, serves as the regulatory molecule. However, this is not a general mechanism affecting all Met4-regulated genes, as MET16 expression is unaffected in a gsh1 mutant, and GSH acts as a poor repressor of MET16 expression compared with methionine. In summary, GSH biosynthesis is regulated in parallel with sulphate assimilation by activity of the Met4 protein, but GSH1-specific mechanisms exist that respond to GSH availability.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.2002.03174.x
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