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  • Electronic Resource  (251)
  • 1990-1994  (251)
  • 1980-1984
  • 1993  (251)
  • Genetics  (251)
  • 101
    Electronic Resource
    Electronic Resource
    A series of yeast shuttle vectors for expression of cDNAs and other DNA sequences (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1299-1308 
    Details
    ISSN: 0749-503X
    Keywords: 2 μm ori plasmid ; directional cDNA cloning ; genetic complementation ; polylinkers ; shuttle vectors ; cDNA libraries ; colE1 replication control ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Expression/shuttle vectors for the yeast Saccharomyces cerevisiae have usually been large plasmids with only one or a small number of sites that are suitable for cloning and expression. We report here the construction and properties of a series of 12 expression vectors with multiple (four to eight) unique sites in their polylinkers which allow directional cloning and expression of DNA sequences under four different promoters. Eleven of these plasmids replicate at high copy number in Escherichia coli, and all have the yeast TRP1 gene, and the 2 μm origin including REP3 sequence, allowing selection and high copy number replication in yeast. Six of the plasmids are designed for the construction and selection of cDNA libraries from various eukaryotic organisms, allowing directional cloning and expression of cDNAs. All of these six have similar polylinkers containing a unique promoter proximal EcoRI site and a unique promoter distal XhoI site, allowing for directional cloning and expression of ‘ZAP’-type cDNAs. cDNAs that complement a wide variety of yeast mutants can be selected from libraries constructed in this way. The four alternative promoters, ADH2, PGK, GAL10 and SV40 were compared for their relative activity, both in E. coli and in yeast. All yeast promoters showed substantial activity in E. coli with ADH2 showing the highest activity. ADH2 also was well-regulated in yeast, showing very high relative activity under derepressing conditions. cDNAs selected by genetic complementation from libraries constructed in these vectors should be easily subclonable into other vectors, allowing expression in different eukaryotic organisms, DNA sequencing or site-directed mutagenesis.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091203
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  • 102
    Electronic Resource
    Electronic Resource
    The international community of yeast genetics and molecular biology, 121-140 (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 121-140 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091308
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  • 103
    Electronic Resource
    Electronic Resource
    The international community of yeast genetics and molecular biology, 201-220 (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 201-220 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091312
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  • 104
    Electronic Resource
    Electronic Resource
    Physical localization of the flocculation gene FLO1 on chromosome I of Saccharomyces cerevisiae (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1-10 
    Details
    ISSN: 0749-503X
    Keywords: Chromosome I ; Flocculation ; FLO1 ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The genetics of flocculation in the yeast Saccharomyces cerevisiae are poorly understood despite the importance of this property for strains used in industry. To be able to study the regulation of flocculation in yeast, one of the genes involved, FLO1, has been partially cloned. The identity of the gene was confirmed by the non-flocculent phenotype of cells in which the C-terminal part of the gene had been replaced by the URA3 gene. Southern blots and genetic crosses showed that the URA3 gene had integrated at the expected position on chromosome I. A region of approximately 2 kb in the middle of the FLO1 gene was consistently deleted during propagation in Escherichia coli and could not be isolated. Plasmids containing the incomplete gene, however, were still able to cause weak flocculation in a nonflocculent strain. The 3′ end of the FLO1 gene was localized at approximately 24 kb from the right end of chromosome I, 20 kb centromere-proximal to PHO11. Most of the newly isolated chromosome I sequences also hybridized to chromosome VIII DNA, thus extending the homology between the right end of chromosome I and chromosome VIII to approximately 28 kb.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090102
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  • 105
    Electronic Resource
    Electronic Resource
    Yeasts have a four-fold variation in ribosomal DNA copy number (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 53-58 
    Details
    ISSN: 0749-503X
    Keywords: rDNA cluster ; pulsed-field electrophoresis ; yeast ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: By employing pulsed-field gel electrophoresis we have determined the size of the rDNA cluster in wild-type yeast strains representing genera of Candida, Kluyveromyces, Pachysolen, Schizosaccharomyces and Torulaspora. Although the genome size of the examined species is similar (12·3-13·9 Mb), at least a four-fold variation has been observed between the lowest amount of rDNA repeats in P. tannophilus (28) and the highest in C. glabrata and S. poombe (〉 115).In two species the rDNA cluster is represented by two loci, residing either in one (S. pombe) or two chromosomes (C. glabrata).
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090107
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  • 106
    Electronic Resource
    Electronic Resource
    Calendar (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 99-99 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: No abstract.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090113
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  • 107
    Electronic Resource
    Electronic Resource
    Current awareness on yeast (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 101-110 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: No abstract.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090114
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  • 108
    Electronic Resource
    Electronic Resource
    Current awareness on yeast (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 205-212 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: No abstract.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090212
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  • 109
    Electronic Resource
    Electronic Resource
    Nuclear pore complex antigens delineate nuclear envelope dynamics in vegetative and conjugating Saccharomyces cerevisiae (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 235-249 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; nuclear pore ; nuclear envelope ; mitosis ; karyogamy ; cell cycle ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In the yeast Saccharomyces cerevisiae, the nucleus undergoes dramatic shape changes during mitosis and mating. We have studied nuclear envelope dynamics during the processes of mitosis and conjugation using nuclear pore complexes as a marker for the nuclear envelope in wild-type cells and several cell-division-cycle (cdc) mutants.Three monoclonal antibodies are described that recognize nuclear pore complex-related antigens in S. cerevisiae. One of these antibodies, RL1, has been extensively characterized by Gerace and colleagues and recognizes nuclear pore complexes in mammalian and amphibian cells. By indirect immunofluorescence of yeast cells, all three antibodies yield a discontinuous nuclear rim stain. All three react with multiple nuclear-enriched proteins in immunoblots, including the nucleoporin protein encoded by the NSP1 gene.When the antibodies were used in immunofluorescence experiments on mating cells, the nuclear pore complex staining pattern proved to be a sensitive indicator of nuclear fusion. Nuclei with closely apposed spindle pole bodies and unfused nuclear envelopes could be readily distinguished. Marked shape changes were observed in nuclei during fusion and segregation of the diploid nucleus into the zygotic bud.In cdc14 and cdc15 mutants that arrest late in mitosis, the elongated nuclear envelope extension that stretches between daughter nuclei during telophase was preserved. In cytokinesis-defective mutants (cdc3, cdc10, cdc11 and cdc12), the elongated nuclear envelope was usually resolved into two daughter nuclei in the absence of cytokinesis. These results indicate that nuclear envelope division is mechanistically distinguishable from chromosome segregation, nucleolar segregation and cytokinesis.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090304
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  • 110
    Electronic Resource
    Electronic Resource
    YMC1, a yeast gene encoding a new putative mitochondrial carrier protein (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 301-305 
    Details
    ISSN: 0749-503X
    Keywords: Chromosome XVI ; mitochondrial carrier ; ARO7 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have cloned and sequenced a Saccharomyces cerevisiae gene coding for a protein with significant similarities to the mitochondrial carrier family. The gene we termed YMC1 (yeast mitochondrial carrier) is located on chromosome XVI, closely downstream of ARO7 encoding chorismate mutase.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090310
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  • 111
    Electronic Resource
    Electronic Resource
    Targeting of a heterologous protein to the cell wall of Saccharomyces cerevisiae (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 399-409 
    Details
    ISSN: 0749-503X
    Keywords: Glucanase-extractable mannoproteins ; mnn9 ; glucomannoproteins ; α-agglutinin ; α-galactosidase ; GPI-anchor ; immobilized enzymes ; immobilization ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The sexual adhesion protein of Saccharomyces cerevisiae MATα cells, α-agglutinin, could not be extracted from the cell wall with hot sodium dodecyl sulfate (SDS), but became soluble after digestion of the cell with laminarinase. This indicates that it is intimately associated with cell wall glucan. A fusion protein was constructed consisting of the signal sequence of yeast invertase, guar α-galactosidase, and the C-terminal half of the α-agglutinin. Most of the fusion protein was incorporated in the cell wall. A small amount could be extracted with SDS, but most of it could only be extracted with laminarinase. On the other hand, cells containing a construct consisting of the signal sequence of invertase and α-galactosidase released most of the α-galactosidase into the medium and all cell wall-associated α-galactosidase was released by SDS. Labelling with antibodies showed that the α-galactosidase part of the fusion protein was exposed on the surface of the cell wall. The results demonstrate that the C-terminal half of the α-agglutinin contains the information needed to incorporate a protein into the cell wall.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090410
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  • 112
    Electronic Resource
    Electronic Resource
    Functional expression of bacterial β-glucuronidase and its use as a reporter system in the yeast Yarrowia lipolytica (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 71-75 
    Details
    ISSN: 0749-503X
    Keywords: Heterologous expression ; β-glucuronidase ; LEU2 promoter ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The use of β-glucuronidase (β-GUS) as a reporter and sensitive detection system for Yarrowia lipolytica was studied. The Escherichia coli gusA gene was expressed under control of the homologous LEU2 promoter in a transcriptional fusion. An NcoI restriction site was introduced at the translational start-ATG, conserving the most favorable context for initiation of translation. The chimeric LEU2′-gusA gene was integrated into the LEU2 locus by homologous recombination. The β-GUS assay was very sensitive and highly reproducible, using the cytosolic fraction or a total cell extract as the source of enzyme. In a leucine-free medium, β-GUS activity was at a high, constant level, independent of growth phase. In transformants grown on complete medium, β-GUS activity was reduced about three-fold, but doubled during logarithmic growth. No intrinsic β-GUS activity was detectable in untransformed Y. lipolytica and no effect of β-GUS expression on growth was obseved. β-GUS-producing Y. lipolytica cells could be directly detected on media plates containing X-gluc (5-bromo-4-chloro-3-indolyl-β-D-glucuronide).
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090109
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  • 113
    Electronic Resource
    Electronic Resource
    QCR9, the nuclear gene encoding a small subunit of the mitochondrial cytochrome bc1 complex, maps to the right arm of chromosome VII in Saccharomyces cerevisiae (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 95-97 
    Details
    ISSN: 0749-503X
    Keywords: Quinol-cytochrome c reductase ; Saccharomyces cerevisiae ; petite ; yeast chromosome VII ; bc1 complex ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We present here mapping data for QCR9, a nuclear gene encoding a subunit of the ubiquinol-cytochrome c oxidoreductase complex. Deletion of QCR9 results in the inability of cells to grow on non-fermentable carbon sources at 37°C. Thus, qcr9 mutants can be scored by growing cells on YPE/G at 37°C, or followed by the URA3 marker, which was inserted when making the qcr9 deletion strain, JDP1. The location of QCR9 on the right arm of chromosome VII with respect to the previously mapped genes ADE3, SER2 and PET54 is given.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090112
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  • 114
    Electronic Resource
    Electronic Resource
    Galactose inhibition of the constitutive transport of hexoses in Saccharomyces cerevisiae (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 111-119 
    Details
    ISSN: 0749-503X
    Keywords: Yeast ; hexose transport ; galactose inhibition ; glycolysis ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The relationship between the pathways of glucose and galactose utilization in Saccharomyces cerevisiae has been studied. Galactose (which is transported and phosphorylated by inducible systems) is a strong inhibitor of the utilization of glucose, fructose and mannose (which have the same constitutive transport and phosphorylation systems). Conversely, all these three hexoses inhibit the utilization of galactose, though with poor efficiency. These cross-inhibitions only occur in yeast adapted to galactose or in galactose-constitutive mutants.The efficiency of galactose as inhibitor is even greater than the efficiencies of each of the other three hexoses to inhibit the utilization of each other. Phosphorylation is not involved in the inhibition and the transport of sugars is the affected step.The cross-inhibitions between galactose and either glucose, fructose or mannose do not implicate utilization of one hexose at the expense of the other, as it occurs in the mutual interactions between the latter three sugars. It seems that, by growing the yeast in galactose, a protein component is synthesized, or alternatively modified, that once bound to either galactose or any one of the other three hexoses (glucose, fructose or mannose), cross-interacts respectively with the constitutive or the inducible transport systems, impairing their function.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090202
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  • 115
    Electronic Resource
    Electronic Resource
    CNE1, a Saccharomyces cerevisiae Homologue of the Genes Encoding Mammalian Calnexin and Calreticulin (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 185-188 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome I ; calnexin homologue ; CNE1 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090209
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  • 116
    Electronic Resource
    Electronic Resource
    The role of ALA-S and ALA-D in regulating porphyrin biosynthesis in a normal and a HEM R+ mutant strain of Saccharomyces cerevisiaeDedicated to Professor Dr Andres O. M. Stoppani on his 75th Birthday. (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 165-173 
    Details
    ISSN: 0749-503X
    Keywords: δ-Aminolevulinate synthase ; δ-aminoleuvulinate dehydratase ; Saccharomyces cerevisiae HEM R+ mutants ; catabolite repression and derepression ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Catabolite repression and derepression on δ-aminolevulinate synthase (ALA-S) and δ-aminolevulinate dehydratase (ALA-D) in a normal yeast strain, D27, and its derived D27/C6 (HEM R+) were investigated. ALA-S and ALA-D activities and intracellular ALA (I-ALA) at different physiological states of the cells were measured. In YPD medium, under conditions of repression and when glucose was exhausted, both strains behaved identically as if the mutation was not expressed. In YPEt medium, however, both ALA-S and ALA-D activities were higher than in YPD, but the I-ALA content and the enzymic activity profiles shown by the two strains were quite different. It appears, therefore, that the mutation causes a deregulation of ALA-S, so that its activity is kept at a high level throughout the cell cycle. This would explain the increased levels of cytochromes present in the mutant. This mutation may affect some regulatory aspect of ALA formation and renders an ALA-S of high activity; moreover, this enzyme species seems to be more stable than in the normal strain.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090207
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  • 117
    Electronic Resource
    Electronic Resource
    Sequence of a cytochrome c gene from Kluyveromyces lactis and its upstream region (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 201-204 
    Details
    ISSN: 0749-503X
    Keywords: Kluyveromyces lactis ; cytochrome c gene ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The complete sequence of a cytochrome c gene from Kluyveromyces lactis including its upstream region is reported. Sequence of the translated open reading frame is discussed in terms of cytochrome c structural requirements. Putative regulatory signals in the upstream region are described and compared with reported sequences which modulate the expression of respiratory-related yeast genes.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090211
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  • 118
    Electronic Resource
    Electronic Resource
    Cloning and sequencing of the URA3 gene of Kluyveromyces marxianus CBS 6556 (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 677-681 
    Details
    ISSN: 0749-503X
    Keywords: Kluyveromyces marxianus ; URA3 gene ; orotidine-5′-phosphate decarboxylase ; leu2 mutant ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The URA3 gene, coding for orotidine-5′-phosphate decarboxylase, from Kluyveromyces marxianus CBS 6556, was isolated from a genomic DNA library. The K. marxianus URA3 gene encodes a protein of 267 amino acids with a calculated molecular weight of 29·3 kDa. Comparison of the K. marxianus protein with the corresponding enzymes of Saccharomyces cerevisiae and Kluyveromyces lactis showed amino acid sequence identifies of 81% and 88%, respectively. Using contour-clamped homogeneous electric field gel electrophoresis, the genomic copy was found to be located on chromosome VI. We have used the cloned gene for the construction of a K. marxianus leu2 mutant. This mutant contains no heterologous sequences, which is essential to make it acceptable for application in the food industry.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090614
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  • 119
    Electronic Resource
    Electronic Resource
    Current awareness on yeast (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 683-690 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: No abstract.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090615
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  • 120
    Electronic Resource
    Electronic Resource
    Molecular characterization of the SEC1 gene of Saccharomyces cerevisiae: Subcellular distribution of a protein required for yeast protein secretion (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 703-713 
    Details
    ISSN: 0749-503X
    Keywords: Exocytosis ; secretion ; secretion mutant ; Sec protein ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Strains of Saccharomyces cerevisiae harbouring temperature-sensitive mutations in the SEC1 and SEC5 genes exhibit an accumulation of post-Golgi secretory vesicles at 37°C. We have cloned a fragment of yeast DNA which carries two distinct genes, one of which complements a sec1 mutation, and the other a sec5 mutation. Genetic tests confirm that the sec1-complementing gene is indeed SEC1, and is essential for cell growth. Nucleotide sequence analysis reveals that the cloned SEC1 gene is the same as a previously sequenced sec1-complementing gene. The SEC1 sequence encodes a protein of 724 amino acids with a predicted molecular mass of 83 kDa. Antibodies purified from a polyclonal antiserum raised against the protein product of the cloned gene recognize a yeast protein of apparent molecular mass 78 kDa which is found in a detergent-resistant association with a rapidly sedimenting yeast subcellular fraction, behaviour which is suggestive of an interaction with a component of the yeast cytoskeleton.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090704
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  • 121
    Electronic Resource
    Electronic Resource
    TA-repeat microsatellites are closely associated with ARS consensus sequences in yeast chromosome III (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 753-759 
    Details
    ISSN: 0749-503X
    Keywords: Microsatellites ; AT-repeats ; ARS ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Microsatellites are repeats of very short sequences of DNA, interspersed in the genome. In this paper, the occurrence of the two-base repeat microsatellites has been investigated in the DNA sequence of yeast chromosome III. Only AT-repeats were found at a significantly high frequency. Some of the regions with the highest concentration of AT-repeats were located and further analysed, showing a close association with the core consensus of autonomously replicating sequences.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090709
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  • 122
    Electronic Resource
    Electronic Resource
    A 12·8 kb segment, on the right arm of chromosome II from Saccharomyces cerevisiae including part of the DUR1, 2 gene, contains five putative new genes (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 797-806 
    Details
    ISSN: 0749-503X
    Keywords: Yeast ; genome ; MCM2 ; MCM3 ; CDC46 ; KRE2 ; KTR1 ; MNT1 ; YUR1 ; DUR1,2 ; protein glycosylation ; lipase ; peroxisomal targeting signal ; DNA replication ; cdc21sp ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A 12 820 bp fragment from the right arm of chromosome II of Saccharomyces cerevisiae was sequenced and analysed. This fragment contains six non-overlapping long open reading frames (ORFs) designated from the centromere- to the telomere-proximal ends as: YBR1441, 1443, 1444, 1445, 1446 and 1448. YBR1441 encodes a polypeptide of 845 amino acids which shares a long consensus domain with products of S. cerevisiae MCM2, MCM3, CDC46 and Schizosaccharomyces pombe cdc21+ genes. These genes are involved in DNA replication. YBR1445 encodes a polypeptide of 404 amino acids which has strong similarity with the S. cerevisiae KRE2/MNT1, YUR1, KTR1 gene products. The KRE2/MNT1 protein is an α-1,2-mannosyltransferase. The product of YBR1444, which encodes a protein of 375 amino acids, presents a lipase signature sequence and a peroxisomal targeting signal. YBR1448, whose sequence extends further on the telomere-proximal end of the fragment, is identical to the 3′ end of the DUR1,2 gene encoding urea amidolyase. The two ORFs, YBR1443 and YBR1446, exhibit no significant similarity with any known gene.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090714
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  • 123
    Electronic Resource
    Electronic Resource
    Analysis of the inducer-responsive CAR1 upstream activation sequence (UASI) and the factors required for its operation (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 835-845 
    Details
    ISSN: 0749-503X
    Keywords: MCM1 ; ARG80 ; ARG81 ; arginase ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Induced production of arginase (CAR1) enzyme activity and steady-state CAR1 mRNA in Saccharomyces cerevisiae requires wild-type ARG80/ARGRI and ARG81/ARGRII gene products. We demonstrate here that these gene products, along with that of the MCM1 gene, are required for the inducer-dependent UASI-A, UASI-B and UASI-C elements to function but they are not required for operation of inducer-independent CAR1 UASC1 or UASC2M. Through the use of single and multiple point mutations, the CAR1 UASI-B and UASI-C elements were demonstrated to be at least 23 bp in length. Moreover, simultaneous mutation of both ends of an elements gave stronger phenotypes than mutations at either end. The center of the element was more sensitive to mutation than were the ends.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090804
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    Linguistic analysis of chromosome III DNA sequence of Saccharomyces cerevisiae (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 889-905 
    Details
    ISSN: 0749-503X
    Keywords: Yeast ; chromosome III ; DNA sequence ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The analysis of the Saccharomyces cerevisiae chromosome III DNA sequence by computer (‘in silico’) permits the definition of its linguistic characteristics. These characteristics include the designation of non-randomly occurring oligonucleotides, their distribution along the chromosome, and the distribution of some particular homopolymers. All these elements may contribute to the understanding of the organization of information on the chromosome.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090809
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  • 125
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    CLG1, a new cyclin-like gene of Saccharomyces cerevisiae (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 929-931 
    Details
    ISSN: 0749-503X
    Keywords: SK18 ; cell cycle: sequence ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A region of chromosome VII adjacent to SKI8 has a 453 amino acid open reading frame whose sequence has significant similarity to that of HCS26, a G1 cyclin. A disruption mutation of this open reading frame has no apparent phenotype under the conditions tested. ORFD, an open reading frame adjacent to the CDC48 gene, is even more similar to HCS26.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090813
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    A data-base of chromosome III of Saccharomyces cerevisiae (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 941-1029 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090902
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  • 127
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    Current awareness on yeast (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1031-1038 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: No abstract.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090903
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  • 128
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    KTR2: A new member of the KRE2 mannosyltransferase gene family (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1057-1063 
    Details
    ISSN: 0749-503X
    Keywords: Mannosyltransferase ; polymerase chain reaction ; protein glycosylation ; cell wall ; chromosome XI ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The KTR2 gene from Saccharomyces cerevisiae was identified by polymerase chain reaction amplification of genomic DNA using primers derived from regions of high homology between the products of three yeast genes, KRE2, YUR1 and KTR1. The product encoded by the KTR2 gene is a predicted type II membrane protein of 425 amino acid residues with a short cytoplasmic N-terminus, a membrane-spanning region and a large lumenal domain containing four potential N-glycosylation sites. Ktr2p has 58% identity with Yur1p, 39% with Ktr1p and 34% with Kre2p. One member of this gene family, KRE2 (also known as MNT1; Häusler and Robbins, 1992), encodes an α-1,2 mannosyltransferase which adds the third mannose onto O-linked glycoprotein side-chains (Häusler et al., 1992). In contrast to KRE2 null mutants, which produce shortened (two-mannose) chains, mutants harboring a KTR2 gene disruption synthesize O-linked chains with the wild-type patterns of five mannose residues. A null mutation in KTR2 leads to partial resistance to killer toxin and hints that KTR2, which encodes a putative mannosyltransferase, is involved in extracellular matrix assembly.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091004
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  • 129
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    Theoretical analysis of the effects of mitotic crossover in large yeast populations (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1093-1098 
    Details
    ISSN: 0749-503X
    Keywords: Population genetics ; mitotic crossover ; mutation ; selection ; diploid yeast ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In a diploid yeast population which is heterozygous for a given marker, A1A2, mitotic crossover (mit. c.o.) between the centromere and the marker will give rise to homozygous daughter cells, A1A1 and A2A2. Since this causes a decrease in the frequency of A1A2 cells, mit. c.o. is an important population genetic process in vegetatively propagated yeast cultures. The effect of mit. c.o. is counteracted by mutations and, in the case of heterosis, by selection. We present a mathematical analysis of these interactions.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091008
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    Mapping of the RIB1 and RIB7 genes involved in the biosynthesis of riboflavin in Saccharomyces cerevisiae (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1099-1102 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; genetic mapping ; RIB1 ; RIB7 ; RPB5 ; biosynthesis of riboflavin ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091009
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  • 131
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    DNA sequence analysis of a 17 kb fragment of yeast chromosome XI physically localizes the MRB1 gene and reveals eight new open reading frames, including a homologue of the KIN1/KIN2 and SNF1 protein kinases (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1149-1155 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; yeast ; chromosome XI ; MBR1 ; protein kinases ; serine-rich protein ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We report in this paper the sequence of a part of chromosome XI of Saccharomyces cerevisiae. This 17 kbp nucleotide sequence represents the right half of cosmid pUKG151 and contains nine open reading frames, YKL453, 450, 449, 448, 445, 443, 442, 441 and the 5′ part of YKL440. YKL440 was previously identified as the MBR1 gene and plays a role in mitochondrial biogenesis. YKL443 is a homologue of the yeast serine-rich protein (SRP1), while YKL453 presents strong homologies with the KIN1/KIN2/SNF1 kinase family. It must be pointed out that the size of this gene is well above average for yeast.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091016
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    RIM2, MSI1 and PGI1 and located within an 8 kb segment of Saccharomyces cerevisiae chromosome II, which also contains the putative ribosomal gene L21 and a new putative essential gene with a leucine zipper motif (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 645-659 
    Details
    ISSN: 0749-503X
    Keywords: Yeast ; genome ; ribosomal protein L21 ; RIM2 ; ATP carrier ; MSI1 ; IRA1 ; GAP ; PGI1 ; glycolytic genes ; leucine zipper ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We report the DNA sequence of an 8 kb segment localized on the right arm of chromosome II from Saccharomyces cerevisiae. The sequence reveals the presence of eight open reading frames (ORFs). Three of them, YBR1402, YBR1405 and YBR1406 are previously sequenced genes, respectively the RIM2 (replication in mitochondria), MSI1 (multicopy suppressor of IRA1 gene) and PGI1 (phosphoglucoisomerase) genes. The predicted product of the ORF YBR1401 could be the putative yeast ribosomal protein L21. A new essential gene, YBR1403, has been identified by disruption; it possesses a leucine zipper motif.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090611
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  • 133
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    Vectors for the inducible overexpression of glutathione S-transferase fusion proteins in yeast (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 715-722 
    Details
    ISSN: 0749-503X
    Keywords: Gene fusion ; protein purification ; glutathione S-transferase ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A rapid and convenient method of protein purification involves creating a fusion protein with glutathione S-transferase (GST) (Smith and Johnson, Gene 67, 31-40, 1988). In this report, we describe two vectors for the conditional expression of GST fusions in Saccharomyces cerevisiae. The parent plasmid is based on a high-copy, galactose-inducible shuttle vector previously described (Baldari et al., EMBO J. 6, 229-243, 1987). We have demonstrated the use of this system by creating fusions between GST and the yeast RAS2 gene. GST-Ras2 fusion proteins undergo the post-translational modifications required for Ras2p to become membrane localized. These vectors provide a useful system for the expression an dpurification of eukaryotic proteins requiring post-translational modification.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090705
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    A comparative study on the transport of L(-)malic acid and other short-chain carboxylic acids in the yeast Candida utilis: Evidence for a general organic acid permease (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 743-752 
    Details
    ISSN: 0749-503X
    Keywords: Candida utilis ; short-chain carboxylic acids ; transport ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Cells of the yeast Candida utilis grown in medium with short-chain mono-, di- or tricarboxylic acids transported L(-)malic acid by two transport systems at pH 3·0. Results indicate that probably a proton symport for the ionized form of the acid and a facilitated diffusion for the undissociated form were present. Dicarboxylic acids such as succinic, fumaric, oxaloacetic and α-ketoglutaric acids were competitive inhibitors of the malic acid for the high-affinity system, suggesting that these acids used the same transport system. In turn, competitive inhibition uptake studies of labelled carboxylic acid in the low-affinity range indicated that this system was non-specific and able to accept not only carboxylic (mono-, di- or tri-) acids but also some amino acids. Additionally, under the same growth conditions, C. utilis produced two mediated transport systems for lactic acid: a proton symport for the anionic form which appeared to be a common monocarboxylate carrier and a facilitated diffusion system for the undissociated acid displaying a substrate specificity similar to that observed for the low-affinity dicarboxylic acid transport. The mediated carboxylic acid transport systems were inducible and subjected to repression by glucose. In glucose-grown cells the undissociated dicarboxylic acids entered the cells slowly by simple diffusion. Repressed glucose-grown cells were only able to produce both transport systems if an inducer, at low concentration (0·5%, w/v), was present during starvation in buffer. This process was inhibited by the presence of cycloheximide indicating that induction requires de novo protein synthesis. If a higher acid concentration was used, only the low-affinity transport system was detectable, showing that the high-affinity system was also repressed by high concentrations of the inducer.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090708
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    Masthead (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993) 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090801
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  • 136
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    Masthead (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993) 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090901
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  • 137
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    Masthead (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993) 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091001
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    The sequence of a 17.5 kb DNA fragment on the left arm of yeast chromosome XI identifies the protein kinase gene ELM1, the DNA primase gene PRI2, a new gene encoding a putative histone and seven new open reading frames (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1379-1384 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome XI ; ELM1 ; PRI2 ; histone ; nif gene ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A 17.5 kb DNA fragment of chromosome XI, located between the genetic loci mif2 and mak11 was sequenced and analysed. Ten open reading frames were identified. Two of them are the previously sequenced genes ELM1 and PRI2, two (YKL253 and YKL256) show homologies to proteins from other organisms and one (YKL262) to yeast and mouse histone.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091212
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  • 139
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    Masthead (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993) 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090101
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  • 140
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    Identification and genetic mapping of CHL genes controlling mitotic chromosome transmission in yeast (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 11-19 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome transmission mutants ; gene mapping ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Eight independent chl (chromosome loss) mutants were isolated using yeast haploid strain disomic for chromosome III. In these mutants, chromosome III is lost during mitosis 50-fold more frequently than in the wild-type strains. chl mutants are also incapable of stable maintenance of circular and linear artificial chromosomes. Seven of the eight mutations are recessive, and one is semidominant. Complementation tests placed these mutants into six complementation groups (chl11 through chl16). Based on tetrad analysis, chl12, chl14 and chl15 correspond to mutations in single nuclear genes. Tetrad analysis of the other mutants was not possible due to poor spore viability. Complementation analysis was also carried out between collection of chl mutants and ctf mutants (chromosome transmission fidelity) (Spencer et al., 1990). The chl3, chl4, chl8, chl12 and chl15 mutants were unable to complement ctf3, ctf17, ctf12, ctf18 and ctf4, respectively. Three CHL genes were mapped by tetrad analysis. The CHL3 gene is placed on the right arm of chromosome XII, between the ILV5 (33·3 cM) and URA4 (21·8 cM) loci. The CHL10 gene is located on the left arm of chromosome VI, 12·5 cM from the centromere. The CHL15 gene is tightly linked to the KAR3 marker of the right arm of chromosome XVI (8·8 cM). The mapping data indicate that these three genes differ from other genes known to affect chromosome stability in mitosis. Therefore, the total number of the CHL genes identified (including those described by us earlier) is 13 (CHL1-CHL10, CHL12, CHL14 and CHL15).
    Additional Material: 5 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090103
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  • 141
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    Human catalase is imported and assembled in peroxisomes of Saccharomyces cerevisiae (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 59-69 
    Details
    ISSN: 0749-503X
    Keywords: Assembly ; human catalase ; peroxisome ; targeting ; S. cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: To study the conservation of peroxisomal targeting signals, we have determined the intracellular localization of human peroxisomal catalase when expressed in yeast. Using immunofluorescence, differential centrifugation and immunoelectron microscopy, we show that the protein is targeted to the peroxisomes of the heterologous cell and assembled in its active tetrameric form. These data show the conservation of the catalase targeting signal and import specificity between human and yeast peroxisomes.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090108
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  • 142
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    In Saccharomyces cerevisiae, protein secretion into the growth medium depends on environmental factors (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 77-84 
    Details
    ISSN: 0749-503X
    Keywords: Yeast ; protein excretion ; physiological modulation ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In the budding yeast Saccharomyces cerevisiae the cell wall, mainly composed of mannoproteins and glucans, constitutes a barrier to protein excretion in the growth medium. In this paper we have studied the effects of different environmental parameters on excretion of Escherichia coli β-galactosidase obtained by exploiting the glucoamylase II signal sequence. Excretion of the unglycosylated β-galactosidase was detectable only in cells grown in rich medium, was affected by temperature (36°C 〉 30°C 〉〉 24°C) and slightly stimulated by reducing agents. On the contrary, glycosylated proteins, such as α-galactosidase and glucoamylase II, were excreted to a good extent under all tested conditions of medium composition, growth temperature and pH. These data indicate that optimization of environmental parameters may help the excretion of heterologous proteins, offering advantages for protein purification.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090110
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  • 143
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    Change in transport activities of vacuoles of the yeast Yarrowia lipolytica during its growth on glucose (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 121-126 
    Details
    ISSN: 0749-503X
    Keywords: Yeast ; vacuole ; H+-ATPase ; citrate transport ; ΔpH ; membrane potential ; growth phase ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Vacuoles were isolated from Yarrowia lipolytica yeast cells taken at various growth phases under carbon or nitrogen limitation. Vacuoles from the cells at the logarithmic growth phase showed a high activity of vacuolar H+-ATPase (0·9-1·1 U/mg protein) and efficiently generated chemical proton gradient and membrane potential across the tonoplast. Ca2+- and citrate transport were found to be maximal at this growth phase. At growth retardation and then in the stationary phase all the parameters studied decreased irrespective of the method of growth limitation. The citrate-transporting activity of vacuoles completely disappeared at growth retardation, also irrespective of the limitation method and irrespective of whether yeast cells overproduced citrate in the culture medium. The citrate-transporting system of Y. lipolytica vacuolar membrane is concluded not to be involved in citrate efflux and this efflux is probably performed by the plasmalemma transport system.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090203
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    The VPH2 gene encodes a 25 kDa protein required for activity of the yeast vacuolar H+-ATPase (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 175-184 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; vacuolar ATPase ; VPH2: VMA12 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Strains bearing the vph2 mutation are defective in vacuolar acidification. The VPH2 gene was isolated from a genomic DNA library by complementation of the zinc-sensitive phenotype of the mutant. Deletion analysis localized the complementing activity to a 1·2 kb DNA fragment. Sequence analysis of this fragment revealed the presence of a single open reading frame that encoded a protein of 215 amino acids. Computer analysis indicated that the protein, which has a predicted molecular mass of 25 286 Daltons, has two distinct membrane-spanning domains. Biochemical studies indicated that strains bearing the vph2 mutation have greatly reduced levels of vacuolar proton pumping and ATPase activity and that the nucleotide binding subunits of the multimeric vacuolar H+-ATPase failed to be correctly targeted to the vacuolar membrane. The vph2 mutant fails to grow on YEP glycerol medium and on media containing 100 mM-CaCl2 or 4 mM-ZnCl2 or buffered to pH 7·5, a phenotype observed in strains carrying deletions in the genes encoding several vacuolar H+-ATPase subunits. The VPH2 gene is identical to the VMA12 gene (T. Stevens and Y. Anraku, personal communication).
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090208
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  • 145
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    Masthead (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993) 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090301
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  • 146
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    Characterization of plasma membrane H+-ATPase from salt-tolerant yeast Candida versatilis (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 213-220 
    Details
    ISSN: 0749-503X
    Keywords: Yeast ; Candida versatilis ; plasma membrane ; H+-ATPase ; salt tolerance ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Plasma membrane was isolated from the salt-tolerant yeast Candida versatilis and the ATPase in plasma membrane was characterized. The ATPase was a typical H+-ATPase with similar properties to the Saccharomyces cerevisiae and Zygosaccharomyces rouxii enzymes. It was reacted with antibody (IgG) raised against S. cerevisiae plasma membrane H+-ATPase. The ATPase activity was not changed by adding NaCl and KCl to the assay solutions, but was increased by NH4+, especially by ammonium sulfate. In vivo stimulation of ATPase activity was observed by the addition of NaCl into the culture medium, as observed in Z. rouxii. No in vivo activation of H+-ATPase by glucose metabolism was observed in C. versatilis cells and the activity was independent of the growth phase, like Z. rouxii and unlike S. cerevisiae cells.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090302
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  • 147
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    Yeast mutants affected in viability upon starvation have a modified phospholipid composition (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 267-277 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; starvation ; phospholipids ; rvs161 suppressors ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Selection of mutations, based on the suppression of rvs161Δ defects, was performed. Ten mutants were obtained, ranged amongst four complementation groups, named SUR1, SUR2, SUR3 and SUR4. All sur mutations also suppress a mutation in another gene, RVS167, indicating that all six genes are involved in the same biological pathway. The sur mutant cells have abnormal morphologies in stationary phase, i.e. dumbbell-like in sur1, sur2 or sur3 strains and multibudded in sur4 strains. Several phenotypic characteristics of the physiological suppressors as well as the rvs161Δ strain itself led us to analyse the phospholipid composition of the mutants. The assays show an overall decrease of the phospholipid amounts and modifications in the relative contents of some phospholipid classes in sur mutant cells.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090306
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  • 148
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    RPB7, one of two dissociable subunits of yeast RNA polymerase II, is essential for cell viability (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 295-299 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The Saccharomyces cerevisiae RNA polymerase II subunit gene RPB7 was isolated and sequenced. RPB7 is a single copy gene whose sequence predicts a 19,000 Dalton protein of 171 amino acids. RPB7 is known to dissociate from RNA polymerase II as an RPB4/RPB7 subcomplex in vitro. RPB7 also appears to interact with RNA polymerase II in a manner dependent upon RPB4, since RNA polymerase II purified from cells lacking RPB4 also lacks RPB7. Previous results have demonstrated that deletion of the RPB4 results in slow growth and cold- and temperature-sensitivity. In contrast, deletion of the RPB7 gene revealed that it is essential for cell growth and viability. Loss of both the RPB4 and the RPB7 genes causes lethality. These results suggest that RPB7 contributes to the function of RNA polymerase II in the absence of RPB4 either in a manner independent of its association with the enzyme or by directly binding to the enzyme in a manner independent of its association with RPB4.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090309
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  • 149
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    Molecular genetics in Saccharomyces kluyveri: The HIS3 homolog and its use as a selectable marker gene in S. kluyveri and Saccharomyces cerevisiae (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 351-361 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces kluyveri ; HIS3 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We cloned the Saccharomyces kluyveri HIS3 homolog, k-HIS3, and made a partial deletion of the gene. The k-HIS3 gene complemented a HIS3 deletion in S. cerevisiae. The DNA sequences of the open reading frames (ORFs) of the HIS3 homologs are 70% identical at the DNA level and 83% identical at the deduced amino acid level. The ORF upstream of the k-HIS3 gene is related to the PET56 gene of S. cerevisiae found upstream of the HIS3 gene of S. cerevisiae. The ORF downstream from the k-HIS3 gene is not related to the DED1 gene found downstream of the HIS3 gene in S. cerevisiae.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090405
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  • 150
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    Peroxisomal amine oxidase of Hansenula polymorpha does not require its SRL-containing C-terminal sequence for targeting (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 331-338 
    Details
    ISSN: 0749-503X
    Keywords: Hansenula polymorpha ; peroxisomes ; amine oxidase ; peroxisomal targeting signal ; homologous recombination ; integration ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Amine oxidase (AMO) is a peroxisomal matrix protein of Hansenula polymorpha, which is induced during growth of the yeast in media containing primary amines as a sole nitrogen source. The deduced amino acid sequence of the protein contains an SRL sequence at nine amino acids from the C-terminus. In this study, we have examined the possible role of the SRL motif in sorting of AMO to peroxisomes by mutating the corresponding gene sequence. For this purpose, we have developed a DNA construct that is specifically integrated into the AMO locus of the H. polymorpha genome, placing the mutant gene under the control of the endogenous AMO promoter and eliminating expression of the wild-type gene. Analysis of a stable transformant, containing the desired gene configuration, showed that mutation of the C-terminal sequence neither interfered with correct targeting of the protein into the peroxisome nor displayed significant effects on its activity. From this, it was concluded that the SRL-containing C-terminus is not essential for peroxisomal targeting of AMO in H. polymorpha.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090403
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  • 151
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    Genetic and physical localization of the acetyl-coenzyme A synthetase gene ACS1 on chromosome I of Saccharomyces cerevisiae (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 419-421 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome I ; genetic mapping ; acetyl-coenzyme A synthetase ; ACS1 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The ACS1 gene, encoding acetyl-coenzyme A synthetase, was mapped genetically at the left arm of chromosome I between pURA3 and PYK1 at 19 and 28 cM respectively. Comparison with the physical map defined a recombinational ‘hot-spot’ in this region in addition to the one between CDC24 and PYK1.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090412
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  • 152
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    A yeast gene encoding a putative RNA helicase of the “DEAD”-box family (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 429-432 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; RNA helicase ; ‘DEAD’-box gene family ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: An unknown open reading frame from Saccharomyces cerevisiae was identified and sequenced. The predicted amino acid sequence shows high homology to the DEAD-box family of proteins. Gene disruption revealed that the gene is not essential for yeast but necessary for normal cell growth.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090414
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  • 153
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    Three yeast genes, PIR1, PIR2 and PIR3, containing internal tandem repeats, are related to each other, and PIR1 and PIR2 are required for tolerance to heat shock (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 481-494 
    Details
    ISSN: 0749-503X
    Keywords: Gene family ; protein with internal repeats ; S. cerevisiae ; heat shock ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We isolated three highly homologous genes, PIR1, PIR2 and PIR3, collectively called the PIR genes. The remarkable feature of their putative amino acid sequence is that they contain a sequence consisting of 18-19 amino acid residues repeated tandemly seven to ten times. Genes homologous to PIR were found in Kluyveromyces lactis and Zygosaccharomyces rouxii but not in Schizosaccharomyces pombe, suggesting that a set of PIR genes plays some role in budding yeast. Bias of codon usage seen in each of the PIR translation products suggests that they are expressed abundantly. The fact that disruption of each gene is viable indicates that none of them is essential. The double disruptants, pir1 pir2, were viable under various conditions, such as higher temperature (37°C) or high salt concentration, but showed a slow-growing phenotype on an agar slab. Furthermore, they were sensitive to heat shock. Addition of a pir3 disruption to the pir1 pir2 double disruptant brought about no phenotypic difference from the original double mutant. PIR1 and PIR3 are closely linked to each other and are on chromosome XI.
    Additional Material: 10 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090504
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  • 154
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    Increased transformation levels in intact cells of Saccharomyces cerevisiae aculeacin A-resistant mutants (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 523-526 
    Details
    ISSN: 0749-503X
    Keywords: Transformation ; aculeacin A ; plasmid DNA ; acr mutants ; plasma membrane ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Several Saccharomyces cerevisiae mutants resistant to the cell wall synthesis inhibitor aculeacin A exhibit higher transformation levels than the parental strain. Mutant acr2 has been studied in more detail. It is transformed up to ten-fold more efficiently than the wild-type strain with episomal, centromeric and integrative plasmids, and dimethyl sulfoxide has an additive effect improving transformation efficiency. Transformation with linear DNA molecules is not as much affected in acr2 cells. The observed effects may be caused by the altered plasma membrane composition of the mutants.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090508
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  • 155
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    Expression of HIV-1 nef in yeast: The 27 kDa nef protein is myristylated and fractionates with the nucleus (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 565-573 
    Details
    ISSN: 0749-503X
    Keywords: HIV-1 ; Nef ; Saccharomyces cerevisiae ; yeast expression ; myristylation ; CUP1 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The nef gene of human immunodeficiency virus type 1 (HIV-1) has been expressed in the yeast Saccharomyces cerevisiae to produce native Nef proteins. The proteins of Mr 27 kDa and 25 kDa, produced by translation from the first and second start codons of the nef gene react with human HIV-1 antisera. Under low-level steady-state expression conditions, Nef27 undergoes myristylation and is targeted to the nuclear fraction while Nef25 is not myristylated and not nuclear localized. When produced rapidly and to high levels, Nef27 is initially present in the cytoplasm as a soluble myristylated protein that later fractionates with the nucleus.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090602
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  • 156
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    A new promoter-probe vector for Saccharomyces cerevisiae using fungal glucoamylase cDNA as the reporter gene (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 599-605 
    Details
    ISSN: 0749-503X
    Keywords: Promoter-probe vector ; Saccharomyces cerevisiae ; amyloglucosidase ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A system is described for the selection of DNA sequences showing promoter activity in the yeast Saccharomyces cerevisiae using a heterologous reporter enzyme which is efficiently secreted by the yeast host. A multicopy shuttle plasmid of the YEp-type was constructed so as to carry multiple unique cloning sites at the 5′ end of the Aspergillus awamori glucoamylase cDNA. Glucoamylase can only be expressed upon insertion at one of these unique cloning sites of a DNA fragment from any source, provided it is endowed with promoter function in S. cerevisiae. As the glucoamylase signal-peptide is functional in S. cerevisiae, the enzyme is efficiently secreted by the yeast transformants. This phenotype can be very easily detected on plate assays and accurately quantified by spectrophotometric analysis of the culture supernatant. Since S. cerevisiae naturally lacks amylolytic activity, any wild-type strain can be used as a host in this system. To evaluate the system, a DNA pool of random fusions was created by ligating sau 3A digested S. cerevisiae genomic DNA to the BglII-linearized vector. The resulting hybrid plasmids were transformed into S. cerevisiae and several transformants secreting glucoamylase to varying degrees were obtained.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090606
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  • 157
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    Purification and characterization of aminopeptidase yspI from Schizosaccharomyces pombe (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 637-644 
    Details
    ISSN: 0749-503X
    Keywords: Fission yeast ; aminopeptidase ; yeast peptidase ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Aminopeptidase yspI was purified to apparent homogeneity from the fission yeast Schizosaccharomyces pombe. The molecular mass of the native enzyme was estimated to be 184 kDa by gel filtration chromatography. A value of 92 kDa was calculated after sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme is thus a dimer with two identical subunits. Optimum pH for cleavage of synthetic aminoacyl-4-nitroanilides is 7·0. Mercury ions, EDTA and chloroquine were found to be potent inhibitors of aminopeptidase yspI activity. Substrate specificity studies indicate that the purified enzyme cleaves L-lysine-4-nitroanilide with high efficiency.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090610
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  • 158
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    Para-aminobenzoate synthase gene of Saccharomyces cerevisiae encodes a bifunctional enzyme (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 669-675 
    Details
    ISSN: 0749-503X
    Keywords: Chromosome XIV ; Saccharomyces cerevisiae ; PABA synthase ; DNA sequencing ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The Saccharomyces cerevisiae gene for para-aminobenzoate (PABA) synthase has been identified based upon its ability to confer sulfonamide resistance when present on a multicopy episomal vector. The 3840 bp DNA sequence fragment reported here contains a 2199 bp open reading frame encoding a 733 amino acid protein with similarity to the two components of PABA synthase described for prokaryotes (Escherichia coli PabA and PabB), suggesting that PABA synthase is bifunctional in yeast. The cloned sequence was confirmed to be PABA synthase by gene disruption. Chromosome gel analysis places the gene for PABA synthase on chromosome XIV.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090613
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  • 159
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    Announcement (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. ii 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: No abstract.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090702
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  • 160
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    Isolation of single yeast cells by optical trapping (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 723-732 
    Details
    ISSN: 0749-503X
    Keywords: Optical trapping ; yeast ; isolation method ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Individual yeast cells can be successfully isolated and recultured on plates with a new isolation method making use of optical trapping with infrared laser light. The cells can be selected on morphological criteria by high resolution microscopy. The isolation device is constructed from two coverslips separated by spacers, in which selected cells are transferred to a plastic capillary, using the optical trap. To test the procedure, selection experiments were done with a mixture of two Saccharomyces cerevisiae strains, distinguishable both in fluorescence microscopy and on agar plates. These experiments showed that only selected cells were isolated, and close to 100% of the isolated stationary-phase cells formed colonies on agar plates, indicating a high recovery. A lower recovery was obtained with exponential-phase cells, possibly because of a higher sensitivity to laser irradiation. Applications for this method may include the isolation of mutants with altered morphology and the isolation of subpopulations of yeast cultures, for their separate investigation or for the initiation of pure cultures.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090706
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  • 161
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    Cloning and sequencing of the Saccharomyces cerevisiae gene LYP1 coding for a lysine-specific permease (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 771-782 
    Details
    ISSN: 0749-503X
    Keywords: Lysine transport ; permease ; S. cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The LYP1 gene of Saccharomyces cerevisiae was cloned by complementation in lysine-permease-deficint recipient yeast cells, and its nucleotide sequence was determined. An open reading frame of 1833 nucleotides was found encoding a polypeptide of 611 amino acids, with a calculated molecular weight of 68 118. Analysis of the deduced primary structure of the protein revealed ten membrane-spanning regions and three potential N-glycosylation sites. Analysis of the deduced sequence of protein LYP1 indicates homology with other yeast amino-acid permeases, in particular with CAN1, and also the lysine-specific permease of Escherichia coli. The strain transformed by a multi-copy plasmid harbouring the LYP1 gene, showed a 20-fold increase in the maximum velocity of lysine uptake over that in the wild type, with no changes in the affinity of the permease for its substrate.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090711
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  • 162
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    Current awareness on yeast (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 807-814 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: No abstract.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090715
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  • 163
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    Regulation of glycolytic enzymes and the crabtree effect in galactose-limited continuous cultures of Saccharomyces cerevisiae (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 787-795 
    Details
    ISSN: 0749-503X
    Keywords: S. cerevisiae ; glucose repression ; carbon metabolism ; continuous culture ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In order to determine whether the changes in the activities and mRNA levels of enzymes involved in intermediary carbon metabolism previously observed in glucose-limited continuous cultures (Sierkstra et al., 1992a) were glucose specific, we have analysed their regulation in a galactose-limited continuous culture of Saccharomyces cerevisiae. The Vmax of the galactose uptake system was shown to be dilution rate (D) dependent, comparable with the high-affinity glucose uptake. The maximum uptake was observed at D 0·2 h-1 (0·25 mmol min-1 per g) and the minimum uptake (0·1 mmol min-1 per g) at D 0·05 h-1 and 0·3 h-1. The aerobic fermentation of galactose occurred at D 0·275-0·3 h-1 which is identical to the results obtained in glucose-limited continuous cultures of this strain. Because galactose is not a repressing carbon source, this demonstrates that the Crabtree effect is not mediated by, or in any way related to glucose repression. Moreover, invertase and hexokinase I mRNA levels (both subject to glucose repression at the transcriptional level) were present when the yeast produced ethanol in galactose- and glucose-limited continuous cultures. In glucose-limited continuous cultures a decrease in alcohol dehydrogenase (I and II) mRNA levels and activity and phosphoglucomutase activity was observed with increasing dilution rates. In addition, at D 0·3 h-1, when the yeast produced ethanol, glucose-6-phosphate dehydrogenase and pyruvate decarboxylase were induced and a decrease in respiration was observed. The fact that the same changes were seen in a galactose-limited culture and that invertase and hexokinase I mRNA levels were present demonstrates that glucose is not specifically involved in the regulation of these enzymes. The changes observed are therefore caused by the growth rate of the organism, the glycolytic flux (e.g. alcohol dehydrogenase) or the overflow metabolism when the yeast produces ethanol (e.g. pyruvate decarboxylase).
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090713
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  • 164
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    The multifunctional regulatory proteins ABF1 and CPF1 are involved in the formation of a nuclease-hypersensitive region in the promoter of the QCR8 gene (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 847-857 
    Details
    ISSN: 0749-503X
    Keywords: yeast ; transcription ; nucleosome positioning ; chromatin structure ; mitochondria ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The abundant DNA-binding proteins ABF1 and CPF1 are members of a family of global regulators with diverse chromosomal functions in the yeast Saccharomyces cerevisiae. Recent evidence suggests that these protein factors may be involved in establishing and maintaining well-defined chromatin structures in promoter regions and other genetic elements. We have investigated the involvement of ABF1 and CPF1 in chromatin organization at the QCR8 gene, encoding subunit VIII of the mitochondrial ubiquinol-cytochrome c oxidoreductase. The promoter region of the QCR8 gene contains overlapping binding sites for ABF1 and CPF1. Nucleosome positioning studies indicate that the QCR8 gene is associated with a phased array of nucleosomes under both catabolite-repressed and derepressed growth conditions. Analysis of binding site mutants reveals that both ABF1 and CPF1 are involved in maintaining a nuclease-hypersensitive region in the QCR8 promoter. The chromatin structure at QCR8 during steady-state growth is, however, mainly dependent on binding of ABF1 to the promoter region. Implications of these findings for the role played by ABF1 and CPF1 in the regulation of mitochondrial biogenesis and other processes important for cell growth and division will be discussed.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090805
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  • 165
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    Isolation and DNA sequence of the STE14 gene encoding farnesyl cysteine: Carboxyl methyltransferase (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 907-913 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We isolated a mutant defective in C-terminal farnesyl cysteine:carboxyl methyltransferase activity from a screen for mutations causing a-specific sterility. A genomic fragment was cloned from a yeast multi-copy library that restored mating. Both the cloned gene and the sterile mutation were allelic to the STE14 gene. A ste14-complementing 2·17 kb BamHI fragment subclone was sequenced and found to encode a 239 amino acid protein with a molecular weight of 27,887 Daltons. The hydrophobicity profile of the methyltransferase reveals the presence of at least five potential transmembrane domains. In comparisons of the C-terminal methyltransferase amino acid sequence with those in the PIR and Swiss protein databases, no significantly similar sequences were found nor were conserved regions from other methyltransferases present.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090810
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  • 166
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    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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  • 167
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    Treatment of yeast cells with wall lytic enzymes is not required to prepare chromosomes for pulsed-field gel analysis (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1053-1055 
    Details
    ISSN: 0749-503X
    Keywords: Chromosome preparations ; pulsed-field gels ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091003
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  • 168
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    Two distinct yeast proteins are related to the mammalian ribosomal polypeptide L7 (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1085-1091 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; Duplication ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The RLP7 gene of Saccharomyces cerevisiae was cloned, sequenced and localized to the right arm of chromosome XIV, close to the centromere. It encodes a predicted polypeptide (RLP7p) of 322 amino acids, with a calculated molecular mass of 36 kDa and an isoelectric point of 9·6. Putative open reading frames very similar to RLP7 are present in two other yeasts, Kluyveromyces lactis and Candida utilis. The RLP7p gene product has significant sequence similarity to the S. cerevisiae YL8 polypeptide of the large ribosomal subunit (Mizuta et al., 1992), itself homologous to the L7 subunit of mammalian ribosomes. However, RLP7p and YL8 do not functionally replace each other, since an rlp7-Δ::HIS3 strain is completely inviable. Judging from its predicted mass, isoelectric point and amino acid sequence, RLP7p does not correspond to any ribosomal component biochemically identified so far in S. cerevisiae, and also differs from all known ribosomal proteins by the low codon usage bias of its gene.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091007
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  • 169
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    Transcriptional regulation by glucose of the yeast PMA1 gene encoding the plasma membrane H+-ATPase (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1075-1084 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; plasma membrane ATPase ; PMA1 ; transcriptional control ; RAP1 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The yeast plasma membrane H+-ATPase generates a membrane electrochemical gradient which is required for the secondary uptake of nutrients. Although the ATPase has previously been shown to be post-translationally regulated in response to the availability of glucose, there has been no evidence to date for transcriptional regulation of the ATPase gene (PMA1). In this work, we have examined the pool of newly synthesized ATPase that accumulates in secretory vesicles en route to the cell surface in the temperature-sensitive secretory mutant sec6-4, and have observed changes in the level of ATPase polypeptide as a function of the glucose concentration in the growth medium. In parallel, there were rapid and reversible changes in the levels of ATPase mRNA. Finally, when cells were grown on a variety of carbon sources, the amount of ATPase polypeptide was proportional to the specific growth rate, suggesting that PMA1 expression is adjusted according to the metabolic state of the cell. These results complement the findings of Capieaux et al. (Capieaux, E., Vignais, M.-L., Sentenac, A. and Goffeau, A. (1989). J. Biol. Chem. 264, 7437-7446), who show that the transcriptional factor TUF/RAP1 binds to upstream activating sequences in the PMA1 gene. Taken together, the results suggest a model in which transcriptional regulation of the ATPase gene by glucose is mediated by TUF/RAP1.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091006
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  • 170
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    The nucleotide sequence of a 2·1 kb fragment from chromosome VI of Saccharomyces cerevisiae identifies a tRNAGly gene, part of a delta element and a palindromic sequence (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1107-1110 
    Details
    ISSN: 0749-503X
    Keywords: Yeast ; Saccharomyces cerevisiae ; chromosome VI ; tRNAGly ; delta element ; diacylglycerol kinase ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The nucleotide sequence was determined of a 2·1 kb DNA fragment located at approximately 35 kb to the right of the centromere of chromosome VI from Saccharomyces cerevisiae. Analysis revealed the presence of a tRNAGLy gene, part of a delta element and a remarkable palindromic sequence. The longest open reading frame found encodes a putative protein of 195 amino acids. Although the fragment was isolated by hybridization to a human diacylglycerol kinase cDNA, no evidence was obtained for the presence of a gene encoding diacylglycerol kinase.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091011
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  • 171
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    The RHO4a and NUD1 genes on Saccharomyces cerevisiae chromosome XI (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1139-1147 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome XI ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Sequence analysis of a 4 kb fragment from the right arm of Saccharomyces cerevisiae chromosome XI, in combination with Northern hybridization experiments revealed the presence of two genes, designated RHO4a and NUD1. The first gene encodes a 32 kDa protein showing significant sequence similarity with members of the ras family. Its 3′-terminal sequence is virtually identical to a sequence published previously as the RHO4 gene [Matsui and Toh-e, Gene 114 (1992), 43-49], which, however, appears to start at an internal ATG codon. The RHO4a sequence also overlaps the 5′-terminal sequence of the RNC1 gene [Chow et al., Nucl. Acids Res. 20 (1992), 5215-5221] proposed to encode the yeast yNucR endo/exonuclease. The remainder of this RNC1 gene overlaps with the 5′-end of the NUD1 gene. However, the RNC1 sequence lacks a portion of 276 bp that in our fragment is part of the intergenic region separating RHO4a and NUD1. From these results we conclude that the proposed RNC1 gene is the result of a cloning artefact and that the yNucR protein is instead encoded by the NUD1 gene.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091015
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  • 172
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    Masthead (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993) 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091101
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  • 173
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    Ultrastructural changes in yeast following heat shock and recovery (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1165-1175 
    Details
    ISSN: 0749-503X
    Keywords: Yeast ; ultrastructure ; heat shock ; mitochondria ; nucleolus ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The effects of heat shock and heat stress on the ultrastructure of Saccharomyces cerevisiae is reported. Following a mild heat shock, referred to as an increase in temperature from 25°C to 37°C for 30 min, we observed contraction of the nucleolus, formation of electron-dense particles (90 nm) in mitochondria and heat-shock granules (30-40 nm) in the cytoplasm. The electron-dense particles in the mitochondria were similar in appearance to those previously reported in plant cells exposed to elevated temperatures. In a heat-sensitive yeast strain, the nucleolus was severely aggregated after a mild heat shock, a treatment which hardly affected relatively more heat-resistant strains. The nucleolus was aggregated in all strains after a more severe heat stress (50°C for 2 or 4 min). When cells were observed during a recovery period after heat stress it was found that nucleolar ultrastructure was regained more rapidly in cells that were previously heat shocked compared to cells that were stressed directly with no prior heat shock.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091103
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  • 174
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    The electrophoretic karyotype of two strains of Candida albicans by transverse alternate field electrophoresis reveals higher number of chromosomes ranging from 1 to 3·5 Mb (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1213-1218 
    Details
    ISSN: 0749-503X
    Keywords: Candida albicans ; chromosome size ; karotype ; pulsed field gel electrophoresis ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The advent of the powerful electrophoretic technique, pulsed field gel electrophoresis, first developed on the yeast Saccharomyces cerevisiæ, has brought a vital impulse to the genetic study on the opportunistic pathogen Candida albicans. We report here on sizing and numbering of Candida chromosomes using transverse alternate field electrophoresis. Our results indicate the occurrence of nine to ten electrophoretic bands (depending on type of Candida strain), that range in approximate size from 1 to 3·5 Mbp, and may account for a higher overall chromosome number, because at least two of these bands appear to be doublets. This number of bands, with smaller size, is considerably higher than previously reported.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091108
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  • 175
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    The 5-aminoimidazole ribonucleotide-carboxylase structural gene of the methylotrophic yeast Pichia methanolica: Cloning, sequencing and homology analysis (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1251-1258 
    Details
    ISSN: 0749-503X
    Keywords: Methylotrophic yeasts ; phosphoribosyl-5-aminoimidazole-carboxylase ; gene homology analysis ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The ADE1 gene of the yeast Pichia methanolica encodes phosphoribosyl-5-aminoimidazole-carboxylase (AIRC, EC 4.1.1.21), which is involved in purine biosynthesis. The gene was cloned by complementation of an ade2 mutation in Saccharomyces cerevisiae and a 3077 nucleotide DNA fragment was sequenced. The sequence possessed a single open reading frame, corresponding to a 543 amino acid sequence. The sequence of this putative protein has been compared to the proteins of homologous genes from S. cerevisiae, Schizosaccharomyces pombe, Escherichia coli, chicken and man. The analysis revealed remarkable homology between yeast AIRCs, while for other proteins homology was limited to defined regions.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091112
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  • 176
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    The DNA sequence analysis of the HAP4-LAP4 region on chromosome XI of Saccharomyces cerevisiae suggests the presence of a second aspartate aminotransferase gene in yeast (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1259-1265 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; yeast ; chromosome XI ; HAP4 ; GFA1 ; LAP4 ; AAT1 ; aspartate aminotransferase ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The nucleotide sequence of a 19 000 base pair region from the left arm of chromosome XI of Saccharomyces cerevisiae has been determined and analysed. It covers the HAP4-GFA1-LAP4 loci already described. As expected HAP4, GFA1 and LAP4 genes have been found and six new open reading frames (ORFs) with a coding capacity of more than 100 amino acid residues have been identified. One of them (YKL461) shows a high degree of identity with an aspartate aminotransferase gene. This raises the question of a second aspartate aminotransferase gene in yeast. A second ORF (YKL462) shows features compatible with a membranous localization. The other ORFs do not show a similarity with any known gene. A member of the highly repetitive ‘CAT’ DNA sequence is present.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091113
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  • 177
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    A series of yeast/Escherichia coli λ expression vectors designed for directional cloning of cDNAs and cre/lox-mediated plasmid excision (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1309-1318 
    Details
    ISSN: 0749-503X
    Keywords: Complementation cloning ; shuttle vectors ; Neurospora crassa cDNA library ; automatic subcloning ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A series of Saccharomyces cerevisiae/Escherichia coli λ/plasmid expression vectors have been constructed which allow easy excision of the plasmid sequences from λ. Features of six are described, and two designated λPG15 and λAD5, are characterized in detail. Transcription of cloned sequences is controlled by the alternative promoters, ADH2, PGK, GAL10 and SV40 early, and by the CYC1 transcriptional terminator. Unique EcoRI and XhoI restriction sites in the intervening polylinker make these λ vectors compatible for directional cloning of ‘ZAP’-synthesized cDNAs. Inserted DNAs have been previously shown to have high levels of the genetic activity in both S. cerevisiae and E. coli, allowing these vectors to be used for genetic complementation in both species. Plasmid recovery from the λ vector is mediated by the activity of the cre-encoded enzyme upon lox sequences flanking the plasmid and adjoining the λ arms. The plasmids contain the yeast 2 μm origin and E. coli pBR322 origin, the URA3 or TRP1 yeast selectable markers, and ampicillin-resistance marker in E. coli. The usefulness of the λPG15 and the λAD5 cloning vectors was demonstrated by constructing large Neurospora crassa cDNA libraries. The λPG15-N. crassa library was used to infect purE, purC and trpC mutants of E. coli, and complemented and/or suppressed prototrophic colonies were selected. The flexibility and power of this system for cloning of cDNAs is discussed.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091204
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  • 178
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    Role of O-acetylhomoserine sulfhydrylase in sulfur amino acid synthesis in various yeasts (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1335-1342 
    Details
    ISSN: 0749-503X
    Keywords: Yeasts ; O-Acetylhomoserine sulfhydrylase ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Mutants defective in O-acetylhomoserine sulfhydrylase (OAH-SHLase) were obtained in five yeast strains representative of different yeast genera: Saccharomyces cerevisiae, Kluyveromyces lactis, Yarrowia lipolytica, Schizosaccharomyces pombe and Trichosporon cutaneum. In vitro, in all five strains, the enzyme also had O-acetylserine (OAS) sulfhydrylase activity so it is a ‘bifunctional’ OAH/OAS-SHLase (Yamagata, 1989). The enzyme was only found to be essential in S. cerevisiae (OAH SHLase-negative mutants are auxotrophs). Its impairment in K. lactis caused a slower growth rate and a decrease of the sulfur amino acid pool. In T. cutaneum only the pool was affected whereas in Y. lipolytica and S. pombe the lesion caused no change in the growth rate nor in the pool. In all strains where OAH SHLase-negative mutants were prototrophs, a monofunctional OAS sulfhydrylase was detected. The results indicate that OAH SHLase may play different physiological roles in various yeasts.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091207
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  • 179
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    Sequencing and functional analysis of a 32 560 bp segment on the left arm of yeast chromosome II. Identification of 26 open reading frames, including the KIP1 and SEC17 genes (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1355-1371 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We report here the DNA sequence of a segment (α1006.13: YBLO5) of chromosome II of Saccharomyces cerevisiae, extending over 32·5 kb. The segment contains 26 open reading frames (ORFs) from YBLO501 to YBLO526. YBL0505 corresponds to the SEC17 gene and YBL0521 to the KIP1 gene. YBL0516 contains an intron, YBL0513 shows homology with the RAT protein phosphatase and YBL0526 contains a zinc-finger motif. Disruption of 14 genes by insertion of a URA3 cassette has been performed and these mutants were analysed for their mating and sporulation ability, and for their growth on different carbon sources. YBL0515 and YBL0526 ORFs seem to be involved in the sporulation process.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091210
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  • 180
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    Current awareness on yeast (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 1387-1394 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: No abstract.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091214
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  • 181
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    The international community of yeast genetics and molecular biology, 41-60 (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 41-60 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091304
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  • 182
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    The international community of yeast genetics and molecular biology, 141-160 (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 141-160 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091309
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  • 183
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    The international community of yeast genetics and molecular biology, 221-240 (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 221-240 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091313
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  • 184
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    The international community of yeast genetics and molecular biology, 281-285 (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 281-285 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320091316
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  • 185
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    Reduced efficiency in the glycosylation of the first sequon of Saccharomyces cerevisiae exoglucanase leads to the synthesis and secretion of a new glycoform of the molecule (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 221-234 
    Details
    ISSN: 0749-503X
    Keywords: Exoglucanase (β)-glucosidase ; secretion ; glycosylation ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In addition to exoglucanases (EXGs) I and II, old cultures of Saccharomyces cerevisiae secreted into the culture medium a new immunologically-related material that exhibited exoglucanase activity. The new exoglucanase (EXGII1/2) was purified from stationary-phase cultures. It turned out to be a glycoprotein whose protein portion was identical to that of the other two isoenzymes in terms of ionic properties, size, amino acid composition and NH2-terminal sequence (25 residues). Disruption of the structural gene encoding EXGs I and II resulted in a strain unable to secrete all three isoenzymes. EXGII1/2 was indistinguishable in terms of molecular weight from the single intermediate detected during the deglycosylation (mediated by endo H) of EXGII by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Thus, the new isoenzyme contains only one of the two slightly elongated mannan inner cores present in enzyme II. Two intermediates were, however, detected when the deglycosylation of EXGII was monitored by ion-exchange chromatography (high-pressure liquid chromatography). Site-directed mutagenesis indicated that the major intermediate, which eluted at about the same position as enzyme II1/2, corresponded to protein molecules carrying the oligosaccharide attached to the Asn of the second sequon, whereas the minor one carried the oligosaccharide in the first potential glycosylation site. Several lines of evidence indicate that EXGII1/2 is a biosynthetic product resulting from an imbalance between the rate of protein synthesis and the glycosylation capabilities of the glycosylation machinery.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090303
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  • 186
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    Sequence of a 7·8 kb segment on the left arm of yeast chromosome XI reveals four open reading frames, including the CAP1 gene, an intron-containing gene and a gene encoding a homolog to the mammalian UOG-1 gene (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 279-287 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We report here the DNA sequence of a segment of chromosome XI of Saccharomyces cerevisiae extending over 7·8 kb. The segment contains four long open reading frames, YKL150, YKL153, YKL155 and YKL156, YKL155 corresponds to the CAP1 gene. YKL153 contains an intron and shows an extremely biased codon usage suggestive of a highly expressed protein. YKL156 is a homolog to UOG-1, an open reading frame associated with the cDNA clone of the mammalian growth/differentiation factor 1. YKL150 reveals common motifs to both the RNA polymerase II elongation factor of Drosophila melanogaster and to the yeast PPR2 gene product.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090307
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  • 187
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    Current awareness on yeast (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 307-314 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: No abstract.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090311
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  • 188
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    Physical localization of yeast CYS3, a gene whose product resembles the rat γ-cystathionase and Escherichia coli cystathionine γ-synthase enzymes (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 363-369 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome I ; sulfur assimilation ; CYS3 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have cloned, sequenced and physically mapped the CYS3 gene of Saccharomyces cerevisiae. This gene can complement the cys3-1 allele, and disruptions at this locus lead to cysteine auxotrophy. The predicted CYS3 product is closely related (46% identical) to the rat cystathionine γ-lyase (Erickson et al., 1990), but differs in lacking cysteine residues. These results provide further evidence that the S288C strain of yeast resembles mammals in synthesizing cysteine solely via a trans-sulfuration pathway. The CYS3 product was found to have strong homology to three other enzymes involved in cysteine metabolism: the Escherichia coli metB and metC products and the S. cerevisiae MET25 gene product. The trans-sulfuration enzymes appears to form a diverged family and carry out related functions from bacteria to mammals.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090406
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  • 189
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    Expression of the glucose oxidase gene from Aspergillus niger in Hansenula polymorpha and its use as a reporter gene to isolate regulatory mutations (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 625-635 
    Details
    ISSN: 0749-503X
    Keywords: Aspergillus niger ; gene expression ; glucose oxidase ; Hansenula polymorpha ; MF-α secretion leader sequence ; methylotrophic yeast ; methanol oxidase promoter ; recombinant protein ; regulatory mutants ; reporter gene ; super-secretion mutant ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The glucose oxidase gene (god) from Aspergillus niger was expressed in Hansenula polymorpha using the methanol oxidase promoter and transcription termination region and the MF-α leader sequence from Saccharomyces cerevisiae to direct secretion. The expression cassette was cloned into the S. cerevisiae vector YEp13 and used to transform H. polymorpha strain A16. In the initial transformants plasmid replication was unstable, but was stabilized by a growth regime consisting of alternating cycles of selective and non-selective growth. The stabilized strain was grown to high cell density by fed-batch fermentation. Upon induction of the MOX promoter, glucose oxidase synthesis was initiated. At the end of the fermentation, the culture density was 76 g dry weight/1 and 108 IU/ml (0·5 g/l or 0·65% dry weight) glucose oxidase was found in the culture medium; a further 86 IU/ml (0·43 g/l or 0·56% dry weight) was recovered from the cell lysate. A plate assay was used to monitor glucose oxidase levels in individual colonies. This was then used to isolate mutants which showed abnormal regulation of god expression or which showed an altered pattern of secretion. One mutant, which showed increased production of glucose oxidase, was grown to high cell density by fed-batch fermentation (100·6 g/l) and produced 445 IU/ml (2·25 g/l or 2·2% dry weight) extracellularly and 76 IU/ml (0·38 g/l or 0·4% dry weight) intracellularly. The mutant thus not only increased total production but exported 83% of the total enzyme made compared to 55% in the parent strain.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090609
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  • 190
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    Masthead (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993) 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090701
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  • 191
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    How many yeast genes code for membrane-spanning proteins? (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 691-702 
    Details
    ISSN: 0749-503X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090703
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  • 192
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    The In Vitro permeability of yeast peroxisomal membranes is caused by a 31 kDa integral membrane protein (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 733-742 
    Details
    ISSN: 0749-503X
    Keywords: Yeasts ; peroxisomes ; Hansenula polymorpha ; peroxisomal membrane ; permeability ; membrane protein ; ΔΨ measurements ; pore-forming protein ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A major 31 kDa integral peroxisomal membrane protein (PMP31) of Hansenula polymorpha was purified to homogeneity from isolated peroxisomal membranes by FPLC after solubilization by Triton X-100. Biochemical analysis indicated that this protein, which showed cross-reactivity with antibodies against the 31 kDa porin of the mitochondrial outer membrane of Saccharomyces cerevisiae, had pore-forming properties. Firstly, proteoliposomes composed of asolectin and purified PMP31 showed selective permeability, determined as the [14C]sucrose/[3H]dextran leakage ratios. Furthermore, the generation of a ΔΨ by potassium diffusion gradients was negatively affected by the presence of PMP31 in asolectin liposomes. A similar effect was observed in proteoliposomes containing purified cytochrome c oxidase as a ΔΨ generating system. Control experiments confirmed that the observed leakage is significant and introduced by the incorporation of PMP31 protein. Selective sucrose leakage was abolished in samples pretreated with glutaraldehyde; an identical effect of glutaraldehyde was, however, not observed for the membrane potential measurements.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090707
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  • 193
    Electronic Resource
    Electronic Resource
    Different signals control the activation of glycolysis in the yeast Saccharomyces cerevisiae (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 761-770 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; activation of glycolysis ; signalling ; cyclic AMP ; fructose-2,6-bisphosphate ; phosphofructokinase ; phosphoglucose isomerase ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The glycolytic pathway in Saccharomyces cerevisiae is activated by fermentable sugars at several steps. Mutants with deletions of genes coding for enzymes of the upper part of glycolysis were used to characterize the triggering mechanisms. Synthesis of fructose-2,6-bisphophate is catalysed by two 6-phosphofructo-2-kinase isoenzymes, one of which is activated by fermentable sugars while synthesis of the second enzyme is induced (Kretschmer and Fraenkel, 1991). Increase in the level of fructose-2, 6-bisphosphate is demonstrated to depend on an internal metabolite upstream of the phosphoglucose isomerase reaction. The signalling process correlates with distinct temporal changes in the concentration of glucose-6-phosphate but not with its absolute level, indicating an adaptational mechanism. It is independent of the uptake and phosphorylation systems used by different sugars. Interestingly, this increase, although delayed, could also be observed in strains lacking the rapid cAMP increase after sugar addition which is thought to be responsible for the activating process. Synthesis of glucose-6-P and fructose-6-P is needed for the complete induction of pyruvate kinase and inactivation of fructose-1,6-bisphosphatase. On the other hand, induction of pyruvate decarboxylase depends mainly on a signal in the lower part of glycolysis.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090710
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  • 194
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    Electronic Resource
    Vector YFRp1 allows transformant selection in Saccharomyces cerevisiae via resistance to formaldehyde (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 783-785 
    Details
    ISSN: 0749-503X
    Keywords: Multicopy vector ; yeast ; formaldehyde ; hyper-resistance ; transformant selection ; vector stability ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Formaldehyde (FA), a chemical with low toxic potential, is used as sole selective agent for transformation in the yeast Saccharomyces cerevisiae. Neither stable auxotrophic markers in recipient cells nor defined synthetic media are needed when multicopy vector YFRp1, containing the yeast SFA gene, is employed for yeast transformation. The SFA gene gives stability to the vector and its yeast (and other) passenger genes when transformants are propagated in complex media supplemented with 3-5 mM-FA. Use of inexpensive FA and non-synthetic, undefined media will lower the cost of yeast transformant propagation considerably and thus make feasible large-volume industrial application of transformants containing YFRp1 derivatives.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090712
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  • 195
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    Rapid identification and characterization of peroxisomal assembly mutants in Yarrowia lipolytica (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 507-517 
    Details
    ISSN: 0749-503X
    Keywords: Peroxisome ; immunofluorescence ; PTS-1 ; electroporation ; yeast ; targeting ; biogenesis ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We describe the isolation and characterization of peroxisomal assembly mutants in the genetically manipulable yeast Yarrowia lipolytica (pay mutants). These mutants were initially identified as oleic acid-non-utilizers by their inability to grow on oleic acid, the utilization of which requires peroxisomal β-oxidation enzymes. Identification of a subset of oleic acid-non-utilizers as pay mutants was obtained by a rapid immunofluorescence procedure using antibodies to the peroxisomal targeting signal Ser-Lys-Leu-CO2H. Punctate structures characteristic of peroxisomes were not detected in pay mutants using this technique. This rapid identification by immunofluorescence should be generally applicable to the selection of peroxisomal assembly mutants in other yeasts. To take advantage of the pay mutant system, we constructed a genomic library in the autonomously replicating vector pINA445 and developed an efficient and rapid electroporation procedure for the functional complementation of these mutants. We have been successful in functionally complementing two independent pay mutants. Molecular analysis of these and other complementing genes will allow for characterization of some of the cellular elements involved in peroxisomal assembly.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090506
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  • 196
    Electronic Resource
    Electronic Resource
    Genes required for derepression of an extracellular glucoamylase gene, STA2, in the yeast Saccharomyces (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 533-541 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; starch utilization ; extracellular glucoamylase ; regulatory mutants ; carbon catabolite (glucose) repression ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A diastatic strain of Saccharomyces cerevisiae producing the STA2-encoded extracellular glucoamylase (GA) in a pronounced glucose-repressible fashion was used as a parent for generating mutants with reduced GA activity under normal conditions of derepression. In addition to mutations in STA2, five other recessive mutations were identified which fell into four complementation groups designated haf1 through haf4. RNA blot analysis suggested that the haf mutations confer defects in STA2 transcription. The haf mutants were pleiotropically defective in utilization of alternative carbon sources and resembled the snf (sucrose non-fermenting) mutants identified previously as unable to derepress the expression of the SUC2 gene encoding invertase. We present evidence strongly suggesting that haf1 = snf2, haf3 = snf1 and haf4 = snf5. By phenotypic criteria, the postulated HAF2 gene (which is none of the SNF genes tested) appears to be similar to SNF2, SNF5 and SNF6, and is possibly a non-redundant extension of this group of functionally related SNF genes.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090510
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  • 197
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    Molecular analysis of HEM6 (HEM12) in Saccharomyces cerevisiae, the gene for uroporphyrinogen decarboxylase (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 613-623 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; heme biosynthesis ; uroporphyrinogen decarboxylase ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: HEM6 (HEM12) in Saccharomyces cerevisiae encodes uroporphyrinogen decarboxylase, the fifth enzyme in the heme biosynthetic pathway. The HEM6 (HEM12) gene was cloned by complementation of heme auxotrophy of a hem6 mutant. Sequence analysis revealed an open reading frame of 1086 nucleotides. The predicted amino acid sequence of HEM6 (HEM12) shows extensive homology to those reported for uroporphyrinogen decarboxylase from mammalian sources. Expression of HEM6 (HEM12) was investigated and was found to increase two-fold in a non-fermentable carbon source. However, HEM6 (HEM12) transcription was unaffected by heme or by intermediates in the heme biosynthetic pathway. In addition, HEM6 (HEM12) expression is not regulated by the transcriptional activator complex HAP2-3-4, as has been shown for some genes encoding heme biosynthetic enzymes.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090608
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  • 198
    Electronic Resource
    Electronic Resource
    Effects of growth with ethanol on fermentation and membrane fluidity of Saccharomyces cerevisiae (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 825-833 
    Details
    ISSN: 0749-503X
    Keywords: Respiration ; fermentation ; glycolysis ; carbon dioxide ; mitochondria ; oxygen ; ethanol tolerance ; yeast ; membrane fluidity ; mass spectrometry ; microsomes ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Saccharomyces cerevisiae HSc was grown with ethanol at concentrations up to 10% (v/v). The immediate effects of additions of externally added ethanol on CO2 production and O2 consumption of washed organisms were studied by stopped-flow membrane inlet quadrupole mass spectrometry. Fermentative activities of organisms grown with ethanol (0-5% v/v) showed similar sensitivities to inhibition by ethanol, whereas those grown with 10% (v/v) ethanol had become protected and were markedly less sensitive.The fluidity of subcellular membrane fractions was measured by determination of the temperature dependence of the rotational order parameter of the spin label 5-doxyl stearic acid (free radical) by electron spin resonance. Mitochondria prepared from yeasts grown with 0, 7 and 9% (v/v) ethanol showed similar overall fluidity, although differences in temperature-dependent behaviour indicate altered lipid composition or lateral phase separations. On the other hand the microsomal fraction from organisms grown with 9% ethanol showed a remarkable increase in fluidity. These data suggest that the protective effects of growth with ethanol near the limit of tolerance on fermentative activities may arise from altered plasma membrane fluidity properties.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090803
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  • 199
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    Electronic Resource
    Metabolic studies of a fructose-intolerant yeast by in vivo 31P-nuclear magnetic resonance spectroscopy (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 867-873 
    Details
    ISSN: 0749-503X
    Keywords: Ketohexokinase ; fructose-intolerance ; sugar phosphates ; 31P-NMR ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The metabolic effects of the administration of fructose to a yeast expressing the cDNA for rat liver ketohexokinase have been investigated by 31P-nuclear magnetic resonance spectroscopy. Cessation of growth suffered by the yeast on exposure to 5 and 25 mM-fructose was accompanied by a large accumulation of fructose 1-phosphate at the expense of cytoplasmic orthophosphate and nucleoside triphosphate. Shifts in resonances were consistent with a drop in cytoplasmic pH. Arresting growth with 1 mM-fructose, however, did not result in these changes, although a large accumulation of fructose 1-phosphate occurred which may have been supported by the mobilization of polyphosphates.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090807
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  • 200
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    Electronic Resource
    Sequence and function analysis of a 4·3 kb fragment of Saccharomyces cerevisiae chromosome II including three open reading frames (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 915-921 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome II ; myo2 suppressor ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The nucleotide sequence of a fragment of 4337 base pairs of Saccharomyces cerevisiae chromosome II has been determined. The sequence contains three open reading frames, one of them being incomplete. Deletion analysis showed that YBR12.31 is essential for yeast growth, while deletion mutants of YBR12.32 and YBR12.33 are viable. YBR12.33 is identical to SMY2, isolated as a suppressor of a myo2 mutant (Lillie, S.H. and Brown, S.S., unpublished, EMBL M90654).
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320090811
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