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  • 1
    ISSN: 1617-4623
    Keywords: CDC25 ; Saccharomyees ; RAS activation ; CAMP signalling
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A potential membrane-interacting site within the essential growth-controlling carboxy-terminal region of the CDC25 protein was interrupted by a lethal mutation (1461 Tyr→Asp and 1462 Leu→Arg). The elimination of two potential phosphorylation sites found in the same region (1489 Thr→Pro and 1584 Ser→Pro) does not affect growth but completely prevents glucose-induced cAMP signalling in the double mutant, whereas the single mutants produce normal or slightly retarded cAMP signals. A cluster of five potential targets for cAMP-dependent phosphorylation at the amino-terminal region could be deleted without affecting phenotypic properties. It is concluded that the carboxy-terminal 137 residues of the CDC25 protein are involved in three different functions: control of mitotic growth, glucose-induced hyperactivation of adenylate cyclase, and feedback inhibition of cAMP synthesis.
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  • 2
    ISSN: 1617-4623
    Keywords: Cell division cycle ; Sporulation ; Gluconeogenesis ; cAMP control pathway ; RAS activation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The cell division cycle gene CDC25 was replaced by various disrupted and deleted mutant copies. Mutants disrupted at a central position of the gene, or lacking 532 residues within the amono-terminal half of the gene product grow normally in glucose, but not in acetate media, and they fail to sporulate as homozygous diploids. Disruptions or deletions within the carboxy-terminal half are lethal, except for the deletion of the 38 carboxy-terminal residues, which are required for sporulation but not for growth in glucose or acetate media. It is concluded that distinct domains of the CDC25 gene product are involved in the control of mitosis and/or meiosis.
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 14 (1998), S. 935-942 
    ISSN: 0749-503X
    Keywords: antifungal drugs ; cytochrome-c oxidase ; gene dosage screening ; lanosterol C-14 demethylase ; overexpression assay ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The post-genome sequencing era of Saccharomyces cerevisiae is defined by the analysis of newly discovered open reading frames of unknown function. In this report, we describe a genetic method for the rapid identification and characterisation of genes involved in a given phenotype. This approach is based on the ability of overexpressed genomic DNA fragments to cure an induced phenotype in yeast. To validate this concept, yeast cells carrying a yeast DNA library present on multicopy plasmid vectors were screened for resistance to the antifungal drug ketoconazole. Among 1·2 million colonies 13 clones tested positive, including those expressing the lanosterol C-14 demethylase, known to be a cellular target for azole drugs, and the cytochrome-c oxidase of mitochondria, regulating the respiratory chain electron transport. Several other resistant clones were identified, which code for yeast proteins of so far unknown function. These genes may represent potential candidates for antifungal drug effects. Together with the availability of the entire yeast genome sequence, the described genetic screening method is a powerful tool for the effective functional analysis of yeast genes. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 4 Ill.
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  • 4
    ISSN: 0730-2312
    Keywords: vitamin D receptor ; retinoid X receptor ; transactivation systems ; vitamin D regulation ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The transcription factors of the nuclear hormone receptor familiy regulate gene expression via a complex network of macromolecular interactions. The ligand dependent activity of the vitamin D receptor is of particular interest because it modulates gene expression by the heterodimeric interaction with retinoid X receptors. We report here that individual functions of the vitamin D receptor including DNA-binding, homo- and heterodimerization and transactivation can be reconstituted in the yeast Saccharomyces cerevisiae. Interestingly, the simultaneous expression of the native vitamin D receptor and the retinoid X receptor β resulted in a ligand independent transactivation of the lacZ reporter gene coupled to a mouse osteopontin vitamin D response element. However, homodimerization of the vitamin D receptor and heterodimerization were strongly enhanced upon ligand binding, when the receptors were expressed as fusion proteins with the Gal4 transcription factor in a yeast two-hybrid system. Furthermore, transactivating activity of a Gal4-fused vitamin D receptor was induced by vitamin D in a one-hybrid system devoid of retinoid X receptors. In addition, both Gal4-based systems behaved similar with regard to their dose-dependent response to vitamin D and related compounds when compared to the transcriptional activity of the vitamin D receptor in transiently transfected MCF-7 cells. Our results point out that specific ligands strongly enhanced receptor dimerization and induced transactivation in yeast and in MCF-7 cells. The constitutive transactivation by vitamin D receptor-retinoid X receptor heterodimers in yeast, depending on DNA binding of the receptors, strongly argues for the existence of cofactors, which are absent in yeast, but play a fundamental role in gene regulation in higher eukaryotic organisms. J. Cell. Biochem. 66:184-196, 1997. © 1997 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
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  • 5
    ISSN: 0730-2312
    Keywords: two-hybrid system ; vitamin D receptor ; retinoid X receptor ; vitamin D ; protein L7 ; basic region leucine zipper domain ; coregulation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The vitamin D receptor (VDR) heterodimerizes with the retinoid X receptor (RXR) and requires additional protein-protein interactions to regulate the expression of target genes. Using the yeast two-hybrid system, we identified the previously described protein L7, that specifically interacted with the VDR in the presence of vitamin D. Deletion analysis indicated, that the N-terminus of L7, which harbours a basic region leucine zipper like domain, mediated interaction with the VDR. Binding assays with purified GST-L7 demonstrated, that L7 specifically pulled down the VDR, that was either expressed in yeast or endogenously contained in the cell line U937. Interestingly, L7 inhibited ligand-dependent VDR-RXR heterodimerization, when constitutively expressed in yeast. We also demonstrate that L7 repressed binding of VDR-RXR heterodimers to a vitamin D response element. Surprisingly, L7 recruited RXR to the same response element in the presence of 9-cis retinoic acid. Ligand-dependent protein-protein interaction in the yeast two-hybrid system confirmed, that binding of L7 also was targeted at the RXR. Our data suggest, that protein L7 is a coregulator of VDR-RXR mediated transactivation of genes, that modulates transcriptional activity by interfering with binding of the receptors to genomic enhancer elements. J. Cell. Biochem. 69:1-12, 1998. © 1998 Wiley-Liss, Inc.
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