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  • 1
    ISSN: 0749-503X
    Keywords: Karyotyping ; Saccharomyces ; biological species ; genetic homology ; cloned genes ; chromosome polymorphism ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Chromosomal DNAs of many monosporic strains of the biological species Saccharomyces cerevisiae, S. paradoxus and S. bayanus were analysed using contour-clamped homogeneous electric field electrophgoresis. SSouthern blot hybridization with eight cloned S. cerevisiae genes (ADC1, CUP1, GAL4, LEU2, rDNA, SUC2, TRP1 and URA3) assigned to different chromosomes was used to study homology and chromosomal location of the genes three sibiling species. A comparative study of Ty1, Ty2 and telomere-associated Y' sequences having multiple chromosomal location was also done.Chromosome length polymorphism was found in cultured strains of S. cerevisiae. Wild S. cerevisiae and S. paradoxus strains yielded chromosome banding patterns very similar to each other, The karyotype pattern of S. bayanus was readily distinguishable from that of S. cerevisiae and S. paradoxus. Southern blot analysis revealed a low degree of homology between the S. cerevisiae genes studied and the corresponding S. paradoxus and S. bayanus genes. The number of chromosomes appears to be 16 in all three species.
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  • 2
    ISSN: 0749-503X
    Keywords: Glycogen phosphorylase ; phosphorylase monomers ; proteinase yscA ; proteolytic modification ; Saccharomyces ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Analyses by sodium dodecyl sulphate-polyacrylamide gradient-gel electrophoresis and Western blotting of the proteins from boiled cell samples from all growth phases of yeast cultures, and from all stages of extract preparation indicate that the smaller subunit (s-monomer), which is found in purified glycogen phosphorylase (EC 2.4.1.1) from baker's yeast, is not present in the living cell. It is observed in extracts of Saccharomyces carlsbergensis and S. cerevisiae after incubation at ambient temperatures or even after storage in the frozen state at -25°C. Its formation is sensitive towards pepstatin A, and it is absent from extracts of several mutants of S. cerevisiae that do not contain active proteinase yscA (EC 3.4.33.6). When purified proteinase yscA-deficient strains are grown with a reduced amount of complex nitrogen compounds, the slightly smaller sc-monomer is formed in their extracts. This event must be attributed to a different proteinase, since it is sensitive towards p-hydroxymercuriphenylsulphonate, but not towards pepstatin A. The N-terminal amino acid of the sc-monomer was found to be blocked, as in the case of the native 1-monomer, but not the s-monomer.
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  • 3
    ISSN: 0749-503X
    Keywords: Saccharomyces ; yeast protein map ; protein identification ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: This publication marks the beginning of the construction of a gene-protein index that relates proteins which are resolved on the two-dimensional protein map of Saccharomyces cerevisiae with their corresponding genes. We report the identification of 36 novel polypeptide spots on the yeast protein map. They correspond to the products of 26 genes. Together with the polypeptide spots previously identified, this raises to 41 the number of genes whose products have been identified on the protein map. The proteins identified here are concerned with four major areas of yeast cellular physiology: carbon metabolism, heat shock, amino acid biosynthesis and purine biosynthesis. Given the molecular weight and isoelectric point of the identified proteins, and the codon-usage bias of the corresponding genes, it can be estimated that 25 to 35% of all the soluble yeast proteins are detectable under the labelling and running gel conditions used in this study.
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  • 4
    ISSN: 0749-503X
    Keywords: Saccharomyces ; redox ; glycerol ; NADH ; shuttle ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Maintenance of a cytoplasmic redox balance is a necessity for sustained cellular metabolism. Glycerol formation is the only way by which Saccharomyces cerevisiae can maintain this balance under anaerobic conditions. Aerobically, on the other hand, several different redox adjustment mechanisms exist, one of these being the glycerol 3-phosphate (G3P) shuttle. We have studied the importance of this shuttle under aerobic conditions by comparing growth properties and glycerol formation of a wild-type strain with that of gut2Δ mutants, lacking the FAD-dependent glycerol 3-phosphate dehydrogenase, assuming that the consequent blocking of G3P oxidation is forcing the cells to produce glycerol from G3P. To impose different demands on the redox adjustment capability we used various carbon sources having different degrees of reduction.The results showed that the shuttle was used extensively with reduced substrate such as ethanol, whereas the more oxidized substrates lactate and pyruvate, did not provoke any activity of the shuttle. However, the absence of a functional G3P shuttle did not affect the growth rate or growth yield of the cells, not even during growth on ethanol. Presumably, there must be alternative systems for maintaining a cytoplasmic redox balance, e.g. the so-called external NADH dehydrogenase, located on the outer side of the inner mitochondrial membrane. By comparing the performance of the external NADH dehydrogenase and the G3P shuttle in isolated mitochondria, it was found that the former resulted in high respiratory rates but a comparably low P/O ratio of 1·2, whereas the shuttle gave low rates but a high P/O ratio of 1·7.Our results also demonstrated that of the two isoforms of NAD-dependent glycerol 3-phosphate dehydrogenase, only the enzyme encoded by GPD1 appeared important for the shuttle, since the enhanced glycerol production that occurs in a gut2Δ strain proved dependent on GPD1 but not on GPD2. © 1998 John Wiley & Sons, Ltd.
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  • 5
    ISSN: 0749-503X
    Keywords: L-Arabinose ; D-xylose ; UDP-glucose 4-epimerase ; inactivation ; Saccharomyces ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In a previous paper (Cármenes et al., 1984) we reported that UDP-glucose 4-epimerase from Saccharomyces was inactivated both in vitro (Crude extracts) by L-arabinose or D-xylose. In this paper, we reported that pure epimerase requires the presence of UMP or UDP to be inactivated by sugars and that the inactivation is due to the reduction of the epimerase NAD+, which is essential for epimerase activity. The inactivation rate is directly proportional to epimerase and sugar concentrations and hyperbolically proportional to UMP concentration. In situ experiments made with permeabilized cells showed that epimerase is inactivated in the same way when it is inside the cell. In vivo studies showed that epimerase is inactivated to a smaller extent when 1% Dgalactose is present in the culture medium than when 1% ethanol is the main carbon source.
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 2 (1986), S. 163-167 
    ISSN: 0749-503X
    Keywords: Shuttle vectors ; gene cloning ; Saccharomyces ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Two yeast/E. coli shuttle vectors have been constructed. The two vectors, YEp351 and YEp352, have the following properties: (1) they can replicate autonomuosly in Saccharomyces cerevisiae and in E. coli; (2) they contain the β-lactamase gene and confer ampicillin resistance to E. coli; (3) they contain the entire sequence of pUC18; (4) all ten restriction sites of the multiple cloning region of pUC18 including EcoRI, SacI, KpnI, SmaI, BamH1, XbaI, SbaI, SalI, PstI, SphI and HindIII are unique in YEp352; these sites are also unique in YEp351 except for EcoRI and KpnI, which occur twice; (5) recombinant plasmids with DNA inserts in the multiple cloning region of YEp351 and YEp352 can be recognised by loss of β-galactosidase function in appropriate E. coli hosts; (6) YEp351 and YEp352 contain the yeast LEU2 and URA3 genes, respectively, allowing for selection of these grown under non-selective conditions indicative of high plasmid copy number. The above properties make the shuttle vectors suitable for constructions of yeast genomic libraries and for cloning of DNA fragments defined by a large number of different restriction sites.The two vectors have been further modified by deletion of the sequences necessary for antunomous replication in yeast. The derivative plasmids YIp651 and YIp352 can therefore be used ti integrate specific sequences into yeast chromosomal DNA.
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  • 7
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 3 (1987), S. 223-232 
    ISSN: 0749-503X
    Keywords: Ethanol tolerance ; membrane fluidity ; fermentation ; Saccharomyces ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Evidence is presented for an exponential increase in yeast plasma membrane fluidity (as meaured by pasive permeability to acetic acid) with ethanol concentration. The role of adaptation of yeast cells to ethanol can be seen in the existence of a threshold concnetration before the onset of an observed fluidizing effect. The physiological state of the yeast cells is also demonstrated to influence the sensitivity of the membrane to fluidizatio by ethanol. On the basis of these results, the concept that increased fluidity is an adaptive response conferring ethanol tolerance is disputed. An alternative hypothesis, namely that the observed increase in fluidity is the net result of a number of more fundamental changes, is presented to explain the observed effects.
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  • 8
    ISSN: 0749-503X
    Keywords: Cell cycle genes ; genetic mapping ; Saccharomyces ; OFAGE ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: CDC3, CDC25 and CDC42 were localized to chromosome XII by hybridizing the cloned genes to Southern blots of chromosomes separated by orthogonal-field-alternation gel electrophoresis. Meiotic tetrad analyses further localized these genes to the region distal to the RDN1 locus on the right arm of the chromosome. The STE11 gene, which had previously been mapped to chromosome XII (Chaleff and Tatchell, 1985), was found to be tightly linked to ILV5. The data suggest a map order of CEN12-RDN1-CDC42-(CDC25-CDC3)-(ILV5-STE11)-URA4. Certain oddities of the data set raise the possibility that there may be constraints on the patterns of recombination in this region of chromosome XII.
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  • 9
    ISSN: 0749-503X
    Keywords: Saccharomyces ; yeast protein map ; protein identification ; mass spectrometry ; Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In this study we used genetically manipulated strains in order to identify polypeptide spots of the protein map of Saccharomyces cerevisiae. Thirty-two novel polypeptide spots were identified using this strategy. They corresponded to the product of 23 different genes. We also explored the possibilities of using peptide-mass fingerprinting for the identification of proteins separated on our gels. According to this strategy, proteins contained in spots are digested with trypsin and the masses of generated peptides are determined by matrix-assisted laser desorption-ionization mass spectrometry (MALDI-MS). The peptide masses are then used to search a yeast protein database for proteins that match the experimental data. Application of this strategy to previously identified polypeptide spots gave evidence of the feasibility of this approach. We also report predictions on the identities of nine unknown spots using MALDI-MS.
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  • 10
    ISSN: 0749-503X
    Keywords: Saccharomyces ; glucose transport ; SNF3 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The SNF3 protein, Snf3p, of Saccharomyces cerevisiae was initially thought to be a high affinity glucose transporter required for efficient catabolism of low glucose concentrations. We now report evidence suggesting that Snf3p is a regulatory protein and not a catabolic transporter. The C-terminal domain of Snf3p is able to complement the growth defect on solid media of snf3 null mutants independent of attachment to the membrane-spanning domains. However, the C-terminal domain is unable to fully restore high affinity glucose transport to a snf3 null strain. Examination of deletions of the C-terminal domain of intact SNF3 demonstrates that this region is required for both the growth and transport functions of Snf3p. Loss of the SNF3 gene leads to a long-term adaptation phenotype for cells grown in liquid medium at low substrate concentrations in the presence of the respiratory inhibitor, antimycin A. The presence of the C-terminal domain shortens the time required for adaptation in a snf3 null strain. Thus, Snf3p appears to affect ability to adapt to low substrate conditions, but does not confer an absolute defect in uptake of substrate. Taken together, these data suggest that Snf3p is a regulatory protein likely functioning in the detection of glucose. © 1997 by John Wiley & Sons, Ltd.
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