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  • ADR1  (2)
  • Cloning vectors  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Monatshefte für Chemie 115 (1984), S. 1229-1235 
    ISSN: 1434-4475
    Keywords: Cloning vectors
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Description / Table of Contents: Zusammenfassung PlasmidpCP1 wurde ausgehend von klonierterSaccharomyces cerevisiae-2 µmDNA und PlasmidpJDB207 konstruiert. Der Vektor enthält die vollständige, imFLP-Gen unterbrocheneB-Form der 2 µmDNA, vomEscherichia coli-Plasmidp AT153 abgeleiteteDNA und eine wenig aktive Variante desS. cerevisiae-LEU2-Gens. Der neue Vektor weist unter nichtselektiven Wachstumsbedingungen incir +- undcir 0-Stämmen eine niedrige Verlustrate auf und ist incir 0-Stämmen stabil gegen Umlagerungen. Seine Verwendbarkeit für die Umwandlung voncir +-Stämmen incir 0-Stämme durch Verdrängung endogener 2 µm-DNA wurde nachgewiesen.
    Notes: Abstract PlasmidpCP1 was constructed from cloned 2 µmDNA ofSaccharomyces cerevisiae and from plasmidpJDB207. VectorpCP1 contains the completeB form of 2 µmDNA interrupted in theFLP gene, together withDNA derived from theEscherichia coli plasmidpAT153 and a low expression variant of theS. cerevisiae LEU2 gene. The new vector is lost at a low frequency from yeastcir + orcir 0 strains under non-selective growth conditions and is stable against rearrangements incir 0 strains. Its usefulness for curingcir + strains from endogenous 2 µmDNA and for their conversion tocir 0 strains was demonstrated.
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  • 2
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Peroxisomes ; Catalase A ; ADR1 ; Peroxisome proliferation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Saccharomyces cerevisiae transcriptional activator ADR1, which controls ADH2 gene expression, was shown to be involved in the regulation of peroxisome proliferation. To study the mode of action of ADR1, we compared strains carrying the adr1-1 mutation, high or low copy numbers of the ADR1 gene, the constitutive allele ADR1-5 c, and 3′-deletions of ADR1. High ADR1 gene dosage increased the transcription of genes encoding peroxisomal proteins as compared to one copy of the ADR1 gene. Furthermore, overexpression of ADR1 under ethanol growth conditions induced the proliferation of peroxisomal structures. The organelles were observed to be localized in clusters, a typical feature of peroxisomes induced by oleic acid. In contrast, the ADR1-5 c allele, which induces ADH2 expression to a level comparable to that of high ADR1 gene dosage was found to have only a small effect. An analysis of functional domains of the ADR1 protein revealed that the N-terminal 220 amino acids of ADR1 were sufficient for wild-type levels of transcription of the FOX2, FOX3, and PAS1 genes, but the entire ADR1 protein was required for complete induction of the CTA1 gene and for growth oleic acid medium. Our data suggest that a functional domain of the ADR1 protein localized between residues 643 and 1323 is required for the induction of peroxisomal structures and for the utilization of oleic acid.
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  • 3
    ISSN: 0749-503X
    Keywords: peroxisome ; Saccharomyces cerevisiae ; ADR1 ; SNF1 ; CAT1 ; CCR1 ; SNF4 ; CAT3 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The Saccharomyces cerevisiae ADR1 gene has recently been demonstrated to control transcription of several genes encoding peroxisomal proteins or proteins necessary for peroxisome formation. Therefore, the effect of two other genes (SNF1 (CAT1, CCR1) and SNF4 (CAT3)) known to control derepression of glucose-repressible genes was studied. Levels of transcripts of genes encoding catalase A, fatty acid β-oxidation enzymes and of the PAS1 gene are reduced in snf1 and snf4 mutants of ethanol as well as on oleic acid medium. By immunogold labelling with an antibody directed against peroxisomal thiolase, clusters of peroxisomes were detected in wild-types cells, whereas smaller single peroxisomes were observed in adr1 mutant cells. Results of immunofluorescence experiments are consistent with these observations. No peroxisomes were detected in snf1 and snf4 mutants by immunogold labelling as well as by imunofluorescence.
    Additional Material: 3 Ill.
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