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  • 1
    Electronic Resource
    Electronic Resource
    Yeast gene YRR1, which is required for resistance to 4-nitroquinoline N-oxide, mediates transcriptional activation of the multidrug resistance transporter gene SNQ2 (1998)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 29 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: We have cloned and characterized a Saccharomyces cerevisiae gene YRR1 that is important for resistance to the mutagen 4-nitroquinoline N-oxide (4-NQO). The wild-type YRR1 gene encodes a protein that contains a Zn(II)2Cys6-type zinc-finger motif. Disruption of the YRR1 gene leads to hypersensitivity to 4-NQO. A dominant mutation (YRR1-1 ) that confers strong resistance to 4-NQO has been identified. Epistasis analysis demonstrated that 4-NQO resistances mediated by the YRR1 and YRR1-1 alleles require the presence of the SNQ2 gene that encodes a multidrug resistance ATP binding cassette superfamily protein responsible for 4-NQO export. Northern blot analysis of SNQ2 mRNA levels indicated that Yrr1p is involved in basal and drug-induced transcriptional activation of SNQ2, whereas Pdr1p/Pdr3p transcription factors are mainly involved in basal SNQ2 expression. In the YRR1-1 mutant, the level of SNQ2 mRNA is constitutively elevated. These results establish that Yrr1p is important for 4-NQO resistance by mediating transcriptional activation of the SNQ2 gene in response to the stress imposed by 4-NQO. The gain-of-function mutation of Yrr1-1p was attributable to the duplication of a 12-amino-acid sequence generated near the carboxy terminus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.01027.x
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  • 2
    Electronic Resource
    Electronic Resource
    Role of calcineurin and Mpk1 in regulating the onset of mitosis in budding yeast (1998)
    [s.l.] : Macmillan Magazines Ltd.
    Nature 392 (1998), S. 303-306 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Signalling via calcium is probably involved in regulating eukaryotic cell proliferation, but details of its mechanism of action are unknown,. In Schizosaccharomyces pombe, the onset of mitosis is determined by activation of a complex of the p34cdc2 protein kinase and a cyclin ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/32695
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  • 3
    Electronic Resource
    Electronic Resource
    Yeast genes involved in growth inhibition by Pseudomonas syringae pv. syringae syringomycin family lipodepsipeptides (1993)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 114 (1993), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract Saccharomyces cerevisiae genes encoding functions necessary for inhibition by the Pseudomonas syringae pv. syringae cyclic lipodepsipeptide, syringomycin-E, were identified by mutant analyses. Syringomycin-E-resistant mutants were isolated, shown to contain single recessive mutations, and divided into eight gene complementation groups. Representative strains from five groups were resistant to nystatin, and deficient in the plasma membrane lipid, ergosterol. All of the mutant strains were resistant to the related cyclic lipodepsipeptides, syringotoxin and syringostatin. The findings show that: 1) at least eight gene-encoded functions participate in the inhibitory response to syringomycin; 2) ergosterol is important for this response; 3) the three related lipodepsipeptides have similar modes of action.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1993.tb06595.x
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  • 4
    Electronic Resource
    Electronic Resource
    Saccharomyces cerevisiae YDR1, which encodes a member of the ATP-binding cassette (ABC) superfamily, is required for multidrug resistance (1994)
    Springer
    Current genetics 26 (1994), S. 285-294 
    Details
    ISSN: 1432-0983
    Keywords: ABC superfamily ; Multidrug resistance ; Saccharomyces cerevisiae ; YDR1 gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A multidrug resistance gene, YDR1, of Saccharomyces cerevisiae, which encodes a 170-kDa protein of a member of the ABC superfamily, was identified. Disruption of YDR1 resulted in hypersensitivity to cycloheximide, cerulenin, compactin, staurosporine and fluphenazine, indicating that YDR1 is an important determinant of cross resistance to apparently-unrelated drugs. The Ydr1 protein bears the highest similarity to the S. cerevisiae Snq2 protein required for resistance to the mutagen 4-NQO. The drug-specificity analysis of YDR1 and SNQ2 by gene disruption, and its phenotypic suppression by the overexpressed genes, revealed overlapping, yet distinct, specificities. YDR1 was responsible for cycloheximide, cerulenin and compactin resistance, whereas, SNQ2 was responsible for 4-NQO resistance. The two genes had overlapping specificities toward staurosporine and fluphenazine. The transcription of YDR1 and SNQ2 was induced by various drugs, both relevant and irrelevant to the resistance caused by the gene, suggesting that drug specificity can be mainly attributed to the functional difference of the putative transporters. The transcription of these genes was also increased by heat shock. The yeast drug-resistance system provides a novel model for mammalian multidrug resistance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00310491
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  • 5
    Electronic Resource
    Electronic Resource
    yAP-1- and yAP-2-mediated, heat shock-induced transcriptional activation of the multidrug resistance ABC transporter genes inSaccharomyces cerevisiae (1996)
    Springer
    Current genetics 29 (1996), S. 103-105 
    Details
    ISSN: 1432-0983
    Keywords: Heat-shock response ; Multidrug resistance ; AP-1 homolog ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have examined whether the stress-induced transcriptional activation ofYDR1/PDR5/STS1 is mediated by yAP-1 and yAP-2. Of the stresses examined, heat shock-induced, rapid and transient PDR5 expression became very low in ayap1 yap2 double-gene disruptant, indicating that the yAP proteins mediate the response. Similar results were obtained withSNQ2, a close homologue ofPDR5. A set of 5′-truncation derivatives of thePDR5 gene identified the region from −484 to −434 as being sufficient for the response. A sequence similar to the yAP-1 recognition element recently identified in the stress-responsive yeast genes was found in this region and in the 5′-flanking sequences ofSNQ2.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02221572
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  • 6
    Electronic Resource
    Electronic Resource
    Topographic and quantitative changes in cell-surface acid-phosphatase during the sexual differentiation of the heterobasidiomycete, Tremella mesenterica (1984)
    Springer
    Archives of microbiology 139 (1984), S. 184-187 
    Details
    ISSN: 1432-072X
    Keywords: Tremella mesenterica ; Sexual differentiation ; Acid phosphatase ; Histochemical staining ; Mating-less mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract During the hormonal induction of the sexual differentiation in the heterobasidiomycetous yeast, Tremella mesenterica, mating type ab cells, the notable increase in acid phosphatase (ACPase) activity was found in cell surface. Electron-microscopic observation by activity straining revealed that the increase in ACPase was specifically occurred at the surface of mating tubes of differentiated cells. The increase in ACPase on cell surface was not induced in all three-types of mating-less mutant strains. Gl-arrest-negative, mating-tube-defective and conjugation-defective strains of ab cells. Thus, it might be concluded that the characteristic arrangement of ACPase caused by sexual differentiation plays a physiological role for cell-cell recognition and/or cell-cell fusion as early events in alteration of generation from vegetative propagation to sexual one.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00401997
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  • 7
    Electronic Resource
    Electronic Resource
    Adaptation to high-salt stress in Saccharomyces cerevisiae is regulated by Ca2+/calmodulin-dependent phosphoprotein phosphatase (calcineurin) and cAMP-dependent protein kinase (1995)
    Springer
    Molecular genetics and genomics 249 (1995), S. 257-264 
    Details
    ISSN: 1617-4623
    Keywords: Calcineurin ; Protein kinase A ; Na+ pump ; Salt tolerance ; Yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Ca2−/calmodulin-dependent phosphoprotein phosphatase (calcineurin, PP2B) of Saccharomyces cerevisiae is implicated in adaptation to high-salt conditions. Calcineurin mediates high salt-induced expression of the ENA1/PMR2 gene encoding the P-type ATPase, which is suggested to be involved in Na+ efflux. We identified the PDE1 gene encoding the low-affinity cAMP phosphodiesterase as a multicopy suppressor of the Li+- and Na+-sensitive calcineurin null mutant, suggesting that cAMP is a negative regulator of adaptation to high-salt stress. Genetic analysis indicated that calcineurin and cAMP act antagonistically in a common pathway for adaptation. The bcy1 disruption, which leads to constitutive cAMP-dependent protein kinase (PKA) activity, inhibited high NaCl-induced expression of the ENA1/PMR2 gene, caused an elevation of the intracellular Na+ level and a growth defect in high-NaCl medium, all of which were analogous to the defects of a calcineurin mutant. A reduced cAMP level resulting from multiple copies of the PDE1 gene caused increased expression of the ENA1/PMR2 gene in response to high NaCl. We propose a model for the regulation of cation homeostasis, in which calcineurin antagonizes PKA to activate transcription of the ENA1/PMR2 gene in response to high-salt conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00290525
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  • 8
    Electronic Resource
    Electronic Resource
    TheSaccharomyces cerevisiae genes (CMP1 andCMP2) encoding calmodulin-binding proteins homologous to the catalytic subunit of mammalian protein phosphatase 2B (1991)
    Springer
    Molecular genetics and genomics 227 (1991), S. 52-59 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Calmodulin-binding protein ; Protein phosphatase (2B type) ; Calcineurin A
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Saccharomyces cerevisiae genomic clones that encode calmodulin-binding proteins were isolated by screening a λgt11 expression library using125I-labeled calmodulin as probe. Among the cloned yeast genes, we found two closely related genes (CMP1 andCMP2) that encode proteins homologous to the catalytic subunit of phosphoprotein phosphatase. The presumed CMP1 protein (62999 Da) and CMP2 protein (68496 Da) contain a 23 amino acid sequence very similar to those identified as calmodulin-binding sites in many calmodulin-regulated proteins. The yeast genes encode proteins especially homologous to the catalytic subunit of mammalian phosphoprotein phosphatase type 213 (calcineurin). The products of theCMP1 andCMP2 genes were identified by immunoblot analysis of cell extracts as proteins of 62000 and 64000 Da, respectively. Gene disruption experiments demonstrated that elimination of either or both of these genes had no effect on cell viability, indicating that these genes are not essential for normal cell growth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00260706
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  • 9
    Electronic Resource
    Electronic Resource
    Stress-induced transcriptional activation mediated by YAP1 and YAP2 genes that encode the Jun family of transcriptional activators in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 250-256 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Transcriptional activator ; AP-1 ; Stress response
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Saccharomyces cerevisiae YAP2 gene encoding an AP-1-like transcriptional activator protein was cloned by selection for genes that confer pleiotropic drug resistance when present in high copy number. The novel YAP2 gene encodes a protein of 45827 daltons and is homologous in part to a known transcriptional activator protein encoded by YAP1/PDR4/SNQ3/PAR1. Homology was found only in both terminal regions. The N-terminal portion contains a region rich in basic amino acids, followed by a “leucine zipper” motif. Overexpression of YAP2 led to the induction of expression of an AP-1 recognition element (ARE)-dependent promoter. The yap1 disruptant has been shown to be sensitive to H2O2. In this study, we demonstrated that the yap1 disruptant is also unable to grow in medium containing 150 μM cadmium, whereas the yap2 disruptant exhibited no significant phenotypes. However, YAP2 in high copy number did suppress cadmium sensitivity, but not H2O2 sensitivity of the yap1 disruptant. YAP1 was able to mediate both cadmium- and H2O2-induced transcriptional activation of an ARE-dependent promoter. A high-copy-number plasmid bearing YAP2 mediated cadmium-induced transcriptional activation of this promoter. The inductions were prevented by the antioxidant N-acetyl-l-cysteine.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00280413
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  • 10
    Electronic Resource
    Electronic Resource
    Isolation and characterization of the nuclei fromSaccharomyces cerevisiae (1981)
    Springer
    Current microbiology 6 (1981), S. 175-180 
    Details
    ISSN: 1432-0991
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract We isolated highly intact nuclei from cells of a haploid strain ofSaccharomyces cerevisiae. The isolated nuclei were spherical, maintained a double membrane with typical nuclear pores, and were free from mitochondrial-, vacuolar-, and cytoplasmic-marker enzymes. The nuclei could synthesize both DNA and RNA and could phosphorylate nuclear proteins in vitro. These biochemical activities were greatly affected by the osmotic treatment of the nuclei.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01642394
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