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  • 1
    Electronic Resource
    Electronic Resource
    Mitochondrial DNA loss by yeast reentry-mutant cells conditionally unable to proliferate from stationary phase (1992)
    Springer
    Current genetics 22 (1992), S. 471-477 
    Details
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; Stationary phase ; mtDNA ; Storage carbohydrate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Double-mutant cells of the budding yeast Saccharomyces cerevisiae harboring the gcs1-1 and sed1-1 mutations are conditionally defective (cold-sensitive) only for reentry into the mitotic cycle from stationary phase. If already proliferating at the permissive temperature (29°C), these reentry-mutant cells continue to proliferate when transferred to the restrictive temperature of 14°C, but under these conditions reentry-mutant cells lose mitochondrial DNA (mtDNA). In addition, upon exhaustion of the nutrient supply at 14°C, these reentry-mutant cells entered stationary phase at a decreased cell concentration and did not accumulate the reserve carbohydrates trehalose and glycogen. Both of these deficiencies were due to the loss of mtDNA, as shown by the responses of wild-type cells also lacking mtDNA. Mitochondrial status did not affect other aspects of the reentry-mutant phenotype. Although mitochondrial activity and the accumulation of carbohydrate reserves are typical features of cells in stationary phase, the reentry-mutant phenotype reveals that neither entry into nor exit from stationary phase need involve mitochondrial function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00326412
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  • 2
    Electronic Resource
    Electronic Resource
    An impaired RNA polymerase II activity in Saccharomyces cerevisiae causes cell-cycle inhibition at START (1993)
    Springer
    Molecular genetics and genomics 241 (1993), S. 327-334 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; RNA polymerase II ; Cyclins ; Transcription ; Cell cycle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Saccharomyces cerevisiae cells harboring the temperature-sensitive mutation rpo21-4, in the gene encoding the largest subunit of RNA polymerase II, were shown to be partially impaired for cell-cycle progress at a permissive temperature, and to become permanently blocked at the cell-cycle regulatory step, START, at a restrictive temperature. The rpo21-4 mutation was lethal in combination with cdc28 mutations in the p34 protein kinase gene required for START. Transcripts of the CLN1 and CLN2 genes, encoding G1-cyclin proteins that, along with p34, are necessary for START, were decreased in abundance by the rpo21-4 mutation at a restrictive temperature. Increased G1-cyclin production, by expression of the CLN1 or CLN2 genes from a heterologous GAL promoter, overcame the rpo21-4 — mediated START inhibition, but such mutant cells nevertheless remained unable to proliferate at a restrictive temperature. These findings reveal that START can be particularly sensitive to an impaired RNA polymerase II function, presumably through effects on G1-cyclin expression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00284685
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Antibodies directed against a yeast carboxyl-terminal peroxisomal targeting signal specifically recognize peroxisomal proteins from various yeasts (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 8 (1992), S. 721-734 
    Details
    ISSN: 0749-503X
    Keywords: Peroxisomes ; protein tarageting ; Saccharomyces cerevisiae ; Candida tropicalis ; Candida albicans ; Yarrowia lipolytica ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The carboxyl-terminal tripeptide Ala-Lys-Ile is essential for targeting Canadida tropicalis trifunctional enzyme (hydratase-dehydrogenase-epimerase) to peroxisomes of both Candida albicans and Saccharomyces cerevisiae (Aitchison, J. D., Murray, W. W. and Rachubinski, R. A. (1991). J. Biol. Chem. 266, 23197-23203). We investigated the possibility that this tripeptide may act as a general peroxisomal targeting signal (PTS) for other proteins in the yeasts C. tropicalis, C. albicans, Yarrowia lipolytica and S. cerevisiae, and in rat liver. Anti-AKI antibodies raised against the carboxyl-terminal 12 amino acids of trifunctional enzyme were used to search for this PTS in proteins of these yeasts and of rat liver. The anti-AKI antibodies reacted exclusively with multiple peroxisomal proteins from the yeasts C. tropicalis, C. albicans and Y. lipolytica. There was a weak reaction of the antibodies with one peroxisomal protein from S. cerevisiae and no reaction with peroxisomal proteins from rat liver. Antibodies directed against a synthetic peptide containing a carboxyl-terminal Ser-Lys-Leu PTS (Gould, S. J., Krisans, S., Keller, G.-A. and Subramani, S. (1990). J. Cell Biol. 110, 27-34) reacted with multiple peroxisomal proteins of rat liver and with peroxisomal proteins of yeast distinct from those identified with anti-AKI antibodies. These results provide evidence that several peroxisomal proteins of different yeasts contain a PTS antigenically similar to that of C. tropicalis trifunctional enzyme and that this signal is absent from peroxisomal proteins from at least one mammalian system, rat liver.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320080905
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  • 4
    Electronic Resource
    Electronic Resource
    Cloning and sequence of ADP-ribosylation factor 1 (ARF1) from Schizosaccharomyces pombe (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 923-927 
    Details
    ISSN: 0749-503X
    Keywords: ADP-ribosylation factors ; GTP-binding proteins ; Saccharomyces cerevisiae ; 3-amniotriazole ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A gene encoding a homologue of the ADP-ribosylation factor (ARF) family of small GTP binding proteins was cloned from a Schizosaccharomyces pombe cDNA library by a functional screen of suppressors of sensitivity to 3-aminotriazole in a gcn3 null strain of Saccharomyces cerevisiae. Two independent isolates each contained the full coding region of the ARF1 gene. The encoded SpARF1 protein has a predicted molecular weight of 20 618 and is 88% and 79% identical to human and S. cerevisiae ARF1 proteins, respectively. As independent isolates were obtained, this effect of the SpARF1 appears to be a real phenomenon, but cannot currently be easily understood within the context of the evidence for a role(s) for ARF proteins in the protein secretory pathway.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090812
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    Paper (German National Licenses)
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