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  • Saccharomyces cerevisiae
  • Wiley-Blackwell  (271)
  • Springer  (243)
  • American Institute of Physics
  • Institute of Physics (IOP)
  • Springer Nature
  • 2010-2014
  • 1990-1994  (514)
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Adaptation of a Saccharomyces cerevisiae strain to high copper concentrations (1994)
    Springer
    BioMetals 7 (1994), S. 221-226 
    Details
    ISSN: 1572-8773
    Keywords: catalase ; copper resistance ; pH-dependent growth ; Saccharomyces cerevisiae ; superoxide dismutase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A strain of Saccharomyces cerevisiae has been adapted to increasing concentrations of copper at two different pH values. The growth curve at pH 5.5 is characterized by a time generation increasing with the amount of added copper. A significant decrease of cell volume as compared with the control is also observed. At pH 3 the cells grow faster than at pH 5.5 and resist higher copper concentrations (3.8 against 1.2 mm). Experimental evidence indicates that, after copper treatment, the metal is not bound to the cell wall, but is localized intracellularly. A significant precipitation of copper salts in the medium was observed only at pH 5.5. Increased levels of superoxide dismutase (SOD) activity were observed in copper-treated cells and which persisted after 20 subsequent inocula in a medium without added metal. On the contrary, catalase activity was not stimulated by copper treatment and, hence, not correlated with SOD levels. The mechanism of copper resistance, therefore, probably involves a persistent induction of SOD, but not of catalase, and it is strongly pH-dependent.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00149552
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  • 2
    Electronic Resource
    Electronic Resource
    Chimeric evolution of the 2-μm genome in Saccharomyces cerevisiae (1994)
    Springer
    Journal of molecular evolution 38 (1994), S. 363-368 
    Details
    ISSN: 1432-1432
    Keywords: Saccharomyces cerevisiae ; 2-μm circle ; DNA sequencing ; Horizontal transmission ; Site-specific recombination ; Selfish DNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We compared the nucleotide substitution pattern over the entire genome of two unique variants of the 6,300-bp selfish DNA (2 μm) plasmid in Saccharomyces cerevisiae. The DNA sequence of the left-unique region is identical among 2-μm variants, while the right-unique region shows substantial divergence. This chimeric pattern cannot be explained by neutral or Darwinian selection models. We propose that horizontal transmission of the 2-μm plasmid coupled with a directed, polarized gene conversion maintains the DNA sequence of the left-unique region, whereas the right-unique region is subject to random drift and Darwinian selection.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00163153
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  • 3
    Electronic Resource
    Electronic Resource
    Mistranslation of human phosphoglycerate kinase in yeast in the presence of paromomycin (1994)
    Springer
    Current genetics 26 (1994), S. 95-99 
    Details
    ISSN: 1432-0983
    Keywords: Translational fidelity ; Paromomycin ; Stuttering ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Missense errors in the translation of mRNAs in Saccharomyces cerevisiae were screened by looking for charge heterogeneity of proteins on two-dimensional gels resulting from the substitution of charged and neutral amino acids. No such mistranslation was detected in wild-type yeast strains grown in the presence of the translational error-inducing antibiotic paromomycin. However, paromomycin-induced mistranslation of a heterologous mRNA, encoding human phosphoglycerate kinase expressed in yeast, was seen. We suggest that the combination of error-prone translation of a heterologous mRNA, and growth in the presence of paromomycin, leads to an accumulation of mistranslated proteins that can be detected by two-dimensional gel electrophoresis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00313794
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  • 4
    Electronic Resource
    Electronic Resource
    Saccharomyces cerevisiae YDR1, which encodes a member of the ATP-binding cassette (ABC) superfamily, is required for multidrug resistance (1994)
    Springer
    Current genetics 26 (1994), S. 285-294 
    Details
    ISSN: 1432-0983
    Keywords: ABC superfamily ; Multidrug resistance ; Saccharomyces cerevisiae ; YDR1 gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A multidrug resistance gene, YDR1, of Saccharomyces cerevisiae, which encodes a 170-kDa protein of a member of the ABC superfamily, was identified. Disruption of YDR1 resulted in hypersensitivity to cycloheximide, cerulenin, compactin, staurosporine and fluphenazine, indicating that YDR1 is an important determinant of cross resistance to apparently-unrelated drugs. The Ydr1 protein bears the highest similarity to the S. cerevisiae Snq2 protein required for resistance to the mutagen 4-NQO. The drug-specificity analysis of YDR1 and SNQ2 by gene disruption, and its phenotypic suppression by the overexpressed genes, revealed overlapping, yet distinct, specificities. YDR1 was responsible for cycloheximide, cerulenin and compactin resistance, whereas, SNQ2 was responsible for 4-NQO resistance. The two genes had overlapping specificities toward staurosporine and fluphenazine. The transcription of YDR1 and SNQ2 was induced by various drugs, both relevant and irrelevant to the resistance caused by the gene, suggesting that drug specificity can be mainly attributed to the functional difference of the putative transporters. The transcription of these genes was also increased by heat shock. The yeast drug-resistance system provides a novel model for mammalian multidrug resistance.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00310491
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  • 5
    Electronic Resource
    Electronic Resource
    Genetic effects of photoactivated psoralens during meiosis in DNA repair mutantpso3-1 ofSaccharomyces cerevisiae (1994)
    Springer
    Current genetics 25 (1994), S. 19-23 
    Details
    ISSN: 1432-0983
    Keywords: Psoralen ; DNA repair mutants ; Gene conversion ; Recombination ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The influence of the DNA repair genePSO3 on photoactivated psoralen-induced meiotic recombination, gene conversion, reverse mutation, and on survival, was assayed in diploid strains ofSaccharomyces cerevisiae homozygous for the wild-type or thepso3-1 mutant allele. Sporulation was normal in thepso3-1 diploid. Wild-type and mutant strains had the same sensitivity to photoactivated monofunctional psoralen (3-CPs+UVA) in meiosis-uncommitted and meiosis-committed stages. The mutant showed higher sensitivity to photoactivated bifunctional psoralen (8-MOP+UVA) during all stages of the meiotic cycle. Mutation induction by 3-CPs+UVA or 8-MOP+UVA in meiosis-committed cells revealed no significant differences between wild-type and thepso3-1 mutant. The status of thePSO3 gene has no influence on the kinetics of induction of gene conversion and crossing-over after 3-CPs+UVA treatment in meiosis-committed cells: gene conversion was blocked while recombination was induced. After treatment with 8-MOP+UVA gene conversion was also blocked in both strains while crossing-over could only be observed in meiosis-committed wild-type cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00712961
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  • 6
    Electronic Resource
    Electronic Resource
    New in-vivo cloning methods by homologous recombination in yeast (1994)
    Springer
    Current genetics 25 (1994), S. 180-183 
    Details
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; In-vivo cloning ; Non-replicative vectors ; Homologous recombination
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have devised a new strategy to clone DNA sequences from an yeast autonomously-propagating plasmid into a non-autonomous integrative vector by in-vivo recombination. The method consists of a first step in which the replicative plasmid carrying the DNA fragment of interest forms a co-integrate with the non-replicative plasmid by an induced in-vivo reciprocal exchange accompanied by gene conversion. The dimeric plasmid obtained is then purified and cut with an appropriate restriction enzyme and ligated independently to obtain the two intact monomeric plasmids, the original autonomous plasmid plus the new non-autonomous plasmid carrying the subcloned DNA fragment. The dimeric co-integrate can also serve as substrate for a second in-vivo reciprocal exchange that produces new autonomous plasmids carrying the desired DNA fragment. The technique considerably expands the applications of in-vivo cloning in yeast by complementing three important characteristics of previously published methods: (1) it can be used to clone into non-propagating vectors; (2) co-transformation experiments are not required; and (3) the intermediate co-integrate can be used to generate new types of autonomously-propagating plasmids directly. These characteristics are independent of whether the DNA insert is flanked by appropriate restriction sites or whether it does, or does not, express a detectable phenotype in yeast. The method is particularly useful for the cloning of large DNA fragments and can be used for plasmids from organisms other than yeasts.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00309546
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  • 7
    Electronic Resource
    Electronic Resource
    Expression of the Saccharomyces cerevisiae CYT2 gene, encoding cytochrome c1 heme lyase (1994)
    Springer
    Current genetics 25 (1994), S. 291-298 
    Details
    ISSN: 1432-0983
    Keywords: Cytochrome c 1 ; Cytochrome c 1 heme lyase ; GRF2p ; Glucose repression ; HAPp ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In this paper we examine the expression of the Saccharomyces cerevisiae CYT2 gene, which encodes cytochrome c 1 heme lyase. This enzyme is required for covalent attachment of heme to apocytochrome c 1, a subunit of the mitochondrial respiratory chain. Transcription of the 1-kb CYT2 mRNA initiates at four prominent sites at a distance of 52–225 bp in front of the AUG start codon. The level of CYT2 mRNA is not influenced by the presence or absence of oxygen or of heme, but it is subject to carbonsource control. The concentration of the CYT2 mRNA is significantly reduced in glucose-grown cells as compared to cells grown under non-repressing conditions. Neither the HAPp activator proteins nor MIG1p, a repressor protein involved in glucose repression, seem to mediate this effect.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00351480
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  • 8
    Electronic Resource
    Electronic Resource
    The Escherichia coli recA gene increases UV-induced mitotic gene conversion in Saccharomyces cerevisiae (1994)
    Springer
    Current genetics 25 (1994), S. 472-474 
    Details
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; recA gene expression ; UV radiation ; Mitotic gene conversion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The effect of the Escherichia coli RecA protein on mitotic recombination in the diploid D7 strain of Saccharomyces cerevisiae damaged by UV radiation was investigated. The D7 strain was transformed by two modified versions of the pNF2 plasmid: one, containing the ADH-1 promoter, and the other containing the recA gene tandemly arranged behind the ADH-1 promoter region. Immunological analysis proved the presence of the 38-kDa RecA protein in D7/pNF2ADHrecA transformants. We observed a positive effect of recA gene expression on mitotic gene conversion, mainly at higher doses of UV radiation. The results indicate that a RecA-like activity could participate in steps preceeding mitotic conversion events in yeast.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00351789
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  • 9
    Electronic Resource
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    ERV1 is involved in the cell-division cycle and the maintenance of mitochondrial genomes in Saccharomyces cerevisiae (1994)
    Springer
    Current genetics 26 (1994), S. 15-20 
    Details
    ISSN: 1432-0983
    Keywords: Cell-division cycle ; Mitochondrial genome ; Nuclear mutation ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In former studies it was found that the ERV1 gene is essential for cell viability and for the biogenesis of functional mitochondria. A temperature-sensitive nuclear mutant exhibits a severe reduction in all the mitochondrial transcripts. Elimination of the gene leads to growth arrest after a few cell divisions. The putative gene product bears the characteristics of a regulatory factor since it has low expression rate and a high content of charged amino acids. In this study it is further verified that the ERV1 gene alone is responsible for the observed cellular and mitochondrial defects. The 5′ region of the gene is analysed by DNA deletions and complementation studies. Expression of the gene under the control of the GAL1-10 promoter in a disruption strain of ERV1 allows a more detailed specification of its influence on mitochondrial and cellular functions. Immediate and complete loss of mitochondrial genomes is observed after the promoter has been shut off, whereas the yeast cells are still able to grow for a limited time under these conditions. Analysis of the cells by in-vivo DNA flurorescence demonstrates a specific arrest in the cell-division cycle as the terminal phenotype. To further characterize the temperature-sensitive allele of ERV1 the mutated gene has been isolated and sequenced. A single point mutation which leads to the exchange of a single amino acid is found in the reading frame.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00326299
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  • 10
    Electronic Resource
    Electronic Resource
    The yeast nuclear gene MRP-L13 codes for a protein of the large subunit of the mitochondrial ribosome (1994)
    Springer
    Current genetics 26 (1994), S. 8-14 
    Details
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; Nuclear gene ; Mitochondria ; Mitochondrial ribosomal protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The nuclear gene MRP-L13 of Saccharomyces cerevisiae, which codes for the mitochondrial ribosomal protein YmL13, has been cloned and characterized. It is a single-copy gene residing on chromosome XI. Its nucleotide sequence was found to be identical to that of the previously reported ORF YK105. A comparison of the predicted protein sequence of the MRP-L13 gene product and the actual N-terminal amino-acid sequence of the isolated YmL13 protein indicated that the mature protein is preceded by a mitochondrial signal peptide of 86 amino-acid residues, which is the longest among all known mitochondrial ribosomal proteins of S. cerevisiae. No sequence similarity was found to any other ribosomal protein in the current databases. The transcription of MRP-L13 was found to be repressed in the presence of glucose. Its protein product is not strictly essential for mitochondrial functions, but disruption of the gene by insertion of LEU2 noticeably affected cellular growth on non-fermentable carbon sources.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00326298
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  • 11
    Electronic Resource
    Electronic Resource
    Antisense RNA regulation of the ILV2 gene in yeast: a correction (1994)
    Springer
    Current genetics 25 (1994), S. 289-289 
    Details
    ISSN: 1432-0983
    Keywords: Saccharomyces cerevisiae ; Inducible antisense gene ; Acetolactate synthase ; Bradytrophic phenocopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A previous report of the use of antisense RNA to regulate gene expression in yeast is incorrect.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00357175
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  • 12
    Electronic Resource
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    Isolation and characterization of three mutants with increased sensitivity to photoactivated 3-carbethoxypsoralen in Saccharomyces cerevisiae (1994)
    Springer
    Current genetics 25 (1994), S. 407-411 
    Details
    ISSN: 1432-0983
    Keywords: Psoralen sensitivity ; Saccharomyces cerevisiae ; DNA repair ; Oxidative stress
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The complementation and genetical analysis of yeast mutants sensitive to photoactivated 3-carbethoxy-psoralen define three novel recessive mutant alleles pso-5-1, pso6-1, and pso7-1. Their cross-sensitivity to UV254nm, radiomimetic mutagens, and to chemicals enhancing oxidative stress suggest that these mutants are either impaired in metabolic steps protecting from oxidative stress or in mechanisms of the repair of oxygen-dependent DNA lesions. None of the three novel mutant alleles block the induction of reverse mutation by photoactivated mono- and bi-functional psoralens, nitrogen mustards, or UV254nm.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00351778
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  • 13
    Electronic Resource
    Electronic Resource
    Suppression of a mitochondrial point mutation in a tRNA gene can cast light on the mechanisms of 3′ end-processing (1994)
    Springer
    Current genetics 25 (1994), S. 451-455 
    Details
    ISSN: 1432-0983
    Keywords: tRNA processing ; Saccharomyces cerevisiae ; Mitochondria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We used a genetic approach to study the nuclear factors involved in the biogenesis of mitochondrial tRNAs. A point mutation in the mitochondrial tRNAAsp gene of Saccharomyces cerevisiae had previously been shown to result in a temperature-sensitive respiratory-deficient phenotype as a result of the absence of 3′ end-processing of the tRNAAsp. Analysis of mitochondrial revertants has shown that all revertants sequenced have a G-A compensatory change at position 53, which restores the hydrogen-bond with the mutated nucleotide. We then searched for nuclear suppressors to identify the nuclear gene(s) involved in mitochondrial tRNA 3′ end-processing. One such suppressor mutation was further characterized: it restores tRNAAsp maturation and growth at 36°C on glycerol medium in heterozygous diploids, but leads to a defective growth phenotype in haploids.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00351785
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  • 14
    Electronic Resource
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    Stabilization of methionine-rich protein in Saccharomyces cerevisiae: targeting of BZN protein into the peroxisome (1994)
    Springer
    Current genetics 26 (1994), S. 390-397 
    Details
    ISSN: 1432-0983
    Keywords: Overexpression ; Peroxisomes ; Saccharomyces cerevisiae ; Stabilization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have constructed a gene coding for the 12-kDa intermediate form of the 2s methionine-rich protein from Bertholletia excelsa seeds. This protein, expressed intracellularly in yeast, is characterised by a 20-min balf-life. By adding 11 amino acids corresponding to the peroxisome-targeting sequence (PTSc) of luciferase, we have significantly increased its half-life. This stabilization allowed accumulation of the BZN protein into the peroxisome as judged by cell fractionation. Accumulation of the 12-kDa protein results in a significant increase of the total methionine content in yeast cells (30%) indicating that such a microorganism could represent a practicable protected shuttl for an animal-feed additive.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00309924
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  • 15
    Electronic Resource
    Electronic Resource
    Sequence analysis of three deficient mutants of cytochrome oxidase subunit I of Saccharomyces cerevisiae and their revertants (1994)
    Springer
    Current genetics 26 (1994), S. 546-552 
    Details
    ISSN: 1432-0983
    Keywords: Cytochrome oxidase ; Revertant ; Mitochondria ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Three respiratory-deficient mutants of cytochrome oxidase subunit I in the yeast mitochondrion have been sequenced. They are located in, or near, transmembrane segment VI, the catalytic core of the enzyme. Respiratory-competent revertants have been selected and studied. The mutant V244M was found to revert at the same site in valine (wild-type), isoleucine or threonine. The revertants of the mutant G251R were of three types: glycine (wild-type), serine and threonine at position 251. A search for second-site mutations was carried out but none were found. Among 60 revertants tested, the mutant K265M was found to revert only to the wild-type allele.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00309948
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  • 16
    Electronic Resource
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    Kinetic studies of killer toxin K1 binding to yeast cells indicate two receptor populations (1994)
    Springer
    Archives of microbiology 162 (1994), S. 211-214 
    Details
    ISSN: 1432-072X
    Keywords: Killer toxin ; Saccharomyces cerevisiae ; Toxin binding ; Cell wall receptor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A recently described new method for determination of killer toxin activity was used for kinetic measurenments of K1 toxin binding. The cells of the killer sensitive strain Saccharomyces cerevisiae S6 were shown to carry two classes of toxin binding sites differing widely in their half-saturation constants and maximum binding rates. The low-affinity and high-velocity binding component (K T1=2.6x109 L.U./ml, V max1=0.19 s-1) probably reflects diffusion-limited binding to cell wall receptors; the high-affinity and low-velocity component (K T2=3.2x107 L.U./ml, V max2=0.03 s-1) presumably indicates the binding of the toxin to plasma membrane receptors. Adsorption of most of the killer toxin K1 to the surface of sensitive cells occured within 1 min and was virtually complete within 5 min. The amount of toxin that saturated practically all cell receptors was about 600 lethal units (L.U.) per cell of S. cerevisiae S6.
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    URL: http://dx.doi.org/10.1007/BF00314477
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  • 17
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    Effect of the new fluorescent brightener Rylux BSU on morphology and biosynthesis of cell walls in Saccharomyces cerevisiae (1994)
    Springer
    Archives of microbiology 161 (1994), S. 340-344 
    Details
    ISSN: 1432-072X
    Keywords: Rylux BSU ; Fluorescent brightener ; Cell walls ; Chitin synthase ; Glucan synthase ; Yeast ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Rylux BSU, a new fluorescent brightener from the family of 4,4′-diaminostilbene-2,2′disulfonic acid derivatives, inhibited growth and cytokinesis of the yeast Saccharomyces cerevisiae. In the presence of 0.1–1 mg/ml Rylux BSU the cells grew in clumps, had irregular shape and were larger than controls. They formed apparently normal primary septa but their secondary septa and lateral cell walls, especially those in older cells, were abnormally thick with large deposits of amorphous wall material in the periplasmic spaces all over the cell surface. Chitin content in the cell walls of cells grown in the presence of Rylux BSU was increased 2 to 5 times in comparison to that of the controls and glucan content was reduced by up to 30%. In the in vitro assays with particulate membrane fractions, Rylux BSU acted as a non-competitive inhibitor of β-1,3-glucan synthase with inhibitory constant K i=1.75 mg/ml whereas the chitin synthase was inhibited to a much lesser extent. From the difference of the effects of Rylux BSU on the synthesis of chitin in vivo and in vitro it is concluded that the brightener interacts with chitin synthase only indirectly, possibly by influencing the properties of integral plasma membrane.
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    URL: http://dx.doi.org/10.1007/BF00303590
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  • 18
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    Kinetic studies of killer toxin K1 binding to yeast cells indicate two receptor populations (1994)
    Springer
    Archives of microbiology 162 (1994), S. 211-214 
    Details
    ISSN: 1432-072X
    Keywords: Key words     Killer toxin ; Saccharomyces cerevisiae ; Toxin binding ; Cell wall receptor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract      A recently described new method for determination of killer toxin activity was used for kinetic measurements of K1 toxin binding. The cells of the killer sensitive strain Saccharomyces cerevisiae S6 were shown to carry two classes of toxin binding sites differing widely in their half-saturation constants and maximum binding rates. The low-affinity and high-velocity binding component (K T1 = 2.6 × 109 L.U./ml, V max1 = 0.19 s– 1) probably reflects diffusion-limited binding to cell wall receptors; the high-affinity and low-velocity component (K T2 = 3.2 × 107 L.U./ml, V max2 = 0.03 s– 1) presumably indicates the binding of the toxin to plasma membrane receptors. Adsorption of most of the killer toxin K1 to the surface of sensitive cells occured within 1 min and was virtually complete within 5 min. The amount of toxin that saturated practically all cell receptors was about 600 lethal units (L.U.) per cell of S. cerevisiae S6.
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    URL: http://dx.doi.org/10.1007/BF00314477
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  • 19
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    Phytate dephosphorylation by free and immobilized cells ofSaccharomyces cerevisiae (1994)
    Springer
    Journal of industrial microbiology and biotechnology 13 (1994), S. 30-34 
    Details
    ISSN: 1476-5535
    Keywords: Phytate ; Saccharomyces cerevisiae ; Polyacrylamide gel ; Inositol phosphates
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Saccharomyces cerevisiae in the form of baker's yeast, cells cultivated on a yeast extract-peptone-glucose medium, as well as cells immobilized in 18% (w/v) polyacrylamide gel showed the ability to hydrolyze 1.727 mM sodium phytate solution at 45°C, pH 4.6, in a stirred tank reactor. Seventy percent yield of dephosphorylation was observed after 2 h using a baker's yeast concentration of 5.8 g dry matter per 100 ml. Hydrolytic activity at 1.8–2.0 μM Pi min−1 was observed between 1st and 3rd h of the reaction in cells cultured 24 or 48 h. No inhibition by the substrate was found at sodium phytate concentrations of 0.587–1.727 mM. After 1.5 h of hydrolysis a single, well distinguished peak ofmyo-inositol-triphosphate was the main product found. By means of immobilization the stability of the biocatalyst was enhanced 3.3-fold and reached its half-life at 64 ninety-minute runs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01569659
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  • 20
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    Evolution of C6, C8 and C10 acids and their ethyl esters in cells and musts during fermentation with threeSaccharomyces cerevisiae races (1994)
    Springer
    Journal of industrial microbiology and biotechnology 13 (1994), S. 269-272 
    Details
    ISSN: 1476-5535
    Keywords: Wine ; Yeasts ; Fatty acids ; Ethyl esters ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary The evolution of the cell and must contents of three short-chain fatty acids (C6, C8 and C10) and their ethyl esters during fermentations withSaccharomyces cerevisiae racescerevisiae, bayanus andcapensis were studied. The former is a fermentative yeast and the last two are ‘flor’ film yeasts. The acid concentrations in the musts increased throughout the alcoholic fermentations, and maximum cell concentrations of the fatty acids were reached after 48 h of fermentation. Maximum ester concentrations in the cells were attained after 48–72 h of fermentation. In the musts, ethyl octanoate and ethyl decanoate reached a peak also at this point, and ethyl hexanoate after 10 days. After 134 days,S. cerevisiae racecapensis formed a thick ‘flor’ film whileS. cerevisiae racebayanus developed a thin film andS. cerevisiae racecerevisiae formed no film. At this point, acid contents remained constant in the wines produced byS. cerevisiae racescerevisiae andbayanus, and decreased in those obtained with racecapensis. The ethyl ester contents tended to decrease with the exception of ethyl decanoate in the fermentations carried out byS. cerevisiae racescerevisiae andbayanus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01569727
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  • 21
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    Isolation and characterization of a multienzyme complex containing DNA replicative enzymes from mitochondria ofS. cerevisiae (1994)
    Springer
    Molecular biology reports 20 (1994), S. 135-141 
    Details
    ISSN: 1573-4978
    Keywords: mitochondria ; multienzyme complex ; replication ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A 40 S multienzyme complex containing mtDNA polymerase was isolated from mitochondria ofS. cerevisiae by density gradient centrifugation and by gel filtration chromatography. Besides DNA polymerase, RNA polymerase, primase, 3′→5′ exonuclease and an ATPase activities were found to be associated with it. The presence of some of these enzymes were confirmed by Western blot. This high molecular weight multienzyme complex containing DNA has most of the attributes of a putative replisome.
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    Cloning of an Arabidopsis thaliana cDNA coding for farnesyl diphosphate synthase by functional complementation in yeast (1994)
    Springer
    Plant molecular biology 26 (1994), S. 1867-1873 
    Details
    ISSN: 1573-5028
    Keywords: Arabidopsis thaliana ; cDNA ; complementation ; erg20-2 yeast mutant ; farnesyl diphosphate synthase ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A cDNA encoding farnesyl diphosphate synthase, an enzyme that synthesizes C15 isoprenoid diphosphate from isopentenyl diphosphate and dimethylallyl diphosphate, was cloned from an Arabidopsis thaliana cDNA library by complementation of a mutant of Saccharomyces cerevisiae deficient in this enzyme. The A. thaliana cDNA was also able to complement the lethal phenotype of the erg20 deletion yeast mutant. As deduced from the full-length 1.22 kb cDNA nucleotide sequence, the polypeptide contains 343 amino acids and has a relative molecular mass of 39689. The predicted amino acid sequence presents about 50% identity with the yeast, rat and human FPP synthases. Southern blot analyses indicate that A. thaliana probably contains a single gene for farnesyl diphosphate synthase.
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    URL: http://dx.doi.org/10.1007/BF00019499
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    Cerulenin-resistant mutants of Saccharomyces cerevisiae with an altered fatty acid synthase gene (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 90-96 
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    ISSN: 1617-4623
    Keywords: Cerulenin ; Saccharomyces cerevisiae ; Fatty acid synthase ; β-Ketoacyl synthase ; Drug resistance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cerulenin, an antifungal antibiotic produced by Cephalosporium caerulens, is a potent inhibitor of fatty acid synthase in various organisms, including Saccharomyces cerevisiae. The antibiotic inhibits the enzyme by binding covalently to the active center cysteine of the condensing enzyme domain. We isolated 12 cerulenin-resistant mutants of S. cerevisiae following treatment with ethyl methanesulfonate. The mechanism of cerulenin resistance in one of the mutants, KNCR-1, was studied. Growth of the mutant was over 20 times more resistant to cerulenin than that of the wild-type strain. Tetrad analysis suggested that all mutants mapped at the same locus, FAS2, the gene encoding the α subunit of the fatty acid synthase. The isolated fatty acid synthase, purified from the mutant KNCR-1, was highly resistant to cerulenin. The cerulenin concentration causing 50% inhibition (IC50) of the enzyme activity was measured to be 400 μM, whereas the IC50 value was 15 μM for the enzyme isolated from the wild-type strain, indicating a 30-fold increase in resistance to cerulenin. The FAS2 gene was cloned from the mutant. Sequence replacement experiments suggested that an 0.8 kb EcoRV-HindIII fragment closely correlated with cerulenin resistance. Sequence analysis of this region revealed that the GGT codon encoding Gly-1257 of the FAS2 gene was altered to AGT in the mutant, resulting in the codon for Ser. Furthermore, a recombinant FAS2 gene, in which the 0.8 Kb EcoRV-HindIII fragment of the wild-type FAS2 gene was replaced with the same region from the mutant, when introduced into FAS2-defective S. cerevisiae complemented the FAS2 pheno-type and showed cerulenin resistance. These data indicate that one amino acid substitution (Gly → Ser) in the α subunit of fatty acid synthase is responsible for the cerulenin resistance of the mutant KNCR-1.
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    Positive and negative transcriptional regulation by the yeast GAL11 protein depends on the structure of the promoter and a combination of cis elements (1994)
    Springer
    Molecular genetics and genomics 245 (1994), S. 301-312 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Transcriptional regulation ; Chromatin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract GAL11 was first identified as a gene required for full expression of some galactose-inducible genes that are activated by GAL4, and it was subsequently shown to be necessary for full expression of another set of genes activated by RAP1/GRFl/TUF. Genetic analysis suggests that GAL11 functions as a coactivator, mediating the interaction of sequence-specific activators with basal transcription factors. To test this hypothesis, we first tried to identify functional domains by deletion analysis and found that the 866–910 region is indispensable for function. Using reporters bearing various upstream activating sequences (UAS) and different core promoter structures, we show that the involvement of GAL11 in transcriptional activation varies with the target promoter and the particular combination of cis elements. Gel electrophoresis in the presence of chloroquine shows that GAL11 affects the chromatin structure of a circular plasmid. Based on these findings, the role of GAL 11 in regulation of transcription, including an alteration in chromatin structure, is discussed.
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    SCM2, a tryptophan permease in Saccharomyces cerevisiae, is important for cell growth (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 260-268 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Amino acid permeases ; Transport ; Tryptophan
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract SCM2, a novel gene encoding a yeast tryptophan permease, was cloned as a high-copy-number suppressor of cse2-1. The cse2-1 mutation causes cold sensitivity, temperature sensitivity and chromosome missegregation. However, only the cold-sensitive phenotype of cse2-1 cells is suppressed by SCM2 at high copy. SCM2 is located on the left arm of yeast chromosome XV, adjacent to SUP3 and encodes a 65 kDa protein that is highly homologous to known amino acid permeases. Four out of five disrupted scm2 alleles (scm2Δ1-Δ4) cause slow growth, whereas one disrupted allele (scm2Δ5) is lethal. Cells with both the scm2Δ1 and trp1-Δ101 mutations exhibit a synthetic cold-sensitive phenotype and grow much more slowly at the permissive temperature than cells with a single scm2Δ1 or trp1-Δ101 mutation. A region of the predicted SCM2 protein is identical to the partial sequence recently reported for the yeast tryptophan permease TAP2, indicating that SCM2 and TAP2 probably encode the same protein.
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    The Saccharomyces cerevisiae SGE1 gene product: a novel drug-resistance protein within the major facilitator superfamily (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 287-294 
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    ISSN: 1617-4623
    Keywords: Drug sensitivity ; Saccharomyces cerevisiae ; Major facilitator superfamily ; Drug expulsion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Several pleiotropic drug sensitivities have been described in yeast. Some involve the loss of putative drug efflux pumps analogous to mammalian P-glycoproteins, others are caused by defects in sterol synthesis resulting in higher plasma membrane permeability. We have constructed a Saccharomyces cerevisiae strain that exhibits a strong crystal violet-sensitive phenotype. By selecting cells of the supersensitive strain for normal sensitivity after transformation with a wild-type yeast genomic library, a complementing 10-kb DNA fragment was isolated, a 3.4-kb subfragment of which was sufficient for complementation. DNA sequence analysis revealed that the complementing fragment comprised the recently sequenced SGE1 gene, a partial multicopy suppressor of gal11 mutations. The supersensitive strain was found to be a sge1 null mutant. Overexpression of SGE1 on a high-copy-number plasmid increased the resistance of the supersensitive strain. Disruption of SGE1 in a wild-type strain increased the sensitivity of the strain. These features of the SGE1 phenotype, as well as sequence homologies of SGE1 at the amino acid level, confirm that the Sge1 protein is a member of the drug-resistance protein family within the major facilitator superfamily (MFS).
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    PDR3, a new yeast regulatory gene, is homologous toPDR1 and controls the multidrug resistance phenomenon (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 501-511 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Transcription factor ; Zinc finger ; Multidrug resistance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract TheSaccharomyces cerevisiae PDR3 gene, located near the centromere of chromosome II, has been completely sequenced and characterised. Mutationspdr3-1 andpdr3-2, which confer resistance to several antibiotics can be complemented by a wild-type allele of the PDR3 gene. The sequence of the wild-typePDR3 gene revealed the presence of a long open reading frame capable of encoding a 976-amino acid protein. The protein contains a single Zn(II)2Cys6 binuclear-type zinc finger homologous to the DNA-binding motifs of other transcriptional activators from lower eukaryotes. Evidence that the PDR3 protein is a transcriptional activator was provided by demonstrating that DNA-bound LexA-PDR3 fusion proteins stimulate expression of a nearby promoter containing LexA binding sites. The use of LexA-PDR3 fusions revealed that the protein contains two activation domains, one localised near the N-terminal, cysteine-rich domain and the other localised at the C-terminus. The salient feature of the PDR3 protein is its similarity to the protein coded byPDR1, a gene responsible forpleiotropicdrugresistance. The two proteins show 36% amino acid identity over their entire length and their zinc finger DNA-binding domains are highly conserved. The fact that the absence of both PDR1 and PDR3 (simultaneous disruption of the two genes) enhances multidrug sensitivity strongly suggests that the two transcriptional factors have closely related functions.
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    Two adjacent nuclear genes, ISF1 and NAM7/UPF1, cooperatively participate in mitochondrial functions in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 49-56 
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    ISSN: 1617-4623
    Keywords: Nuclear suppressor gene ; Mitochondrial functions ; Glucose repression ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We previously isolated a nuclear 5.7 kb genomic fragment carrying the NAM7/UPF1 gene, which is able to suppress mitochondrial splicing deficiency when present in multiple copies. We show here that an immediately adjacent gene ISF1 (Increasing Suppression Factor) increases the efficiency of the NAM7/UPF1 suppressor activity. The ISF1 gene has been independently isolated as the MBR3 gene and comparison of the ISF1 predicted protein sequence with data libraries revealed a significant similarity with the MBRI yeast protein. The ISF1 and NAM7 genes are transcribed in the same direction, and RNase mapping allowed the precise location of their termini within the intergenic region to be determined. The ISF1 gene is not essential for cell viability or respiratory growth. However as for many mitochondrial genes, ISF1 expression is sensitive to fermentative repression; in contrast expression of the NAM7 gene is unaffected by glucose. We propose that ISF1 could influence the NAM7/UPF1 function, possibly at the level of mRNA turnover, thus modulating the expression of nuclear genes involved in mitochondrial biogenesis.
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    Characterization of the Saccharomyces cerevisiae nuclear gene CYB3 encoding a cytochrome b polypeptide of respiratory complex II (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 708-716 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Mitochondria ; Cytochrome b ; Complex II ; HAP2/3/4
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Computer-assisted structural analysis of the predicted product of the previously described open reading frame (ORF) YKL4 located on the left arm of chromosome XI of Saccharomyces cerevisiae revealed a high degree of similarity (〉50%) to bovine cytochrome b 560, the sdhC polypeptide of the Escherichia coli succinate dehydrogenase (SDH) complex and the protein specified by ORF137 located on the chloroplast DNA of Marchantia polymorpha. Disruption of the yeast gene severely impaired mitochondrial function, while Northern analysis showed it to be subject to catabolite repression. Deletion analysis of the CYB3 promoter identified a single HAP2/3/4-binding element that is necessary and sufficient for carbon source-dependent transcriptional regulation. These experiments also suggested the presence of additional, as yet unidentified, transcriptional control elements, both negative and positive. Taken together, these data lead us to conclude that the CYB3 gene encodes the yeast homolog of the bovine cytochrome b 560 component of complex II of the mitochondrial electron transport chain.
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    Functional analysis of the zinc cluster domain of the CYP1 (HAP1) complex regulator in heme-sufficient and heme-deficient yeast cells (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 699-707 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; CYP1(HAP1) protein ; Electron transport ; Oxygen and heme regulation ; Trans regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract CYP1 determines the expression of several genes whose transcription is heme-dependent in yeast. It exerts regulatory functions even in the absence of heme, usually considered to be its effector. It mediates both positive and negative effects, depending on the target gene and on the redox state of the cell. In the presence of heme, it binds through a cysteine-rich domain in which a histidine residue occupies the position of the sixth and essential cysteine of the otherwise classical zinc cluster DNA-binding domain exemplified by GAL4. We constructed specific missense mutations in the potential CYP1 zinc cluster domain by site-directed mutagenesis and looked for regulatory effects of the mutated proteins under specific physiological conditions. We show that CYP1 does belong to the zinc cluster regulatory family since a sixth essential cysteine residue is indeed present, albeit at a modified position when compared to the consensus sequence. We also show that the amino acid preceding the first cysteine residue of the DNA-binding domain critically affects the efficiency of regulation both in the presence and in the absence of heme: mutations known to affect DNA binding under heme-sufficient conditions also affect regulation under heme-deficient conditions. We therefore surmise that regulation under hemedeficient conditions is dependent upon DNA binding.
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    MBR1 and MBR3, two related yeast genes that can suppress the growth defect of hap2, hap3 and hap4 mutants (1994)
    Springer
    Molecular genetics and genomics 243 (1994), S. 575-583 
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    ISSN: 1617-4623
    Keywords: Multicopy suppressors ; HAP2/3/4 activation complex ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two new yeast genes, named MBR1 and MBR3, were isolated as multicopy suppressors of the growth defect of a strain lacking the HAP2 transcriptional activator. Both genes when overexpressed can also suppress the growth defect of hap3 and hap4 null mutants. However, overexpression of MBRI cannot substitute for the HAP2/3/4 complex in activation of the CYC1 gene. Nucleotide sequencing of MBR1 and MBR3 revealed that these two genes encode serine-rich, hydrophilic proteins with regions of significant homology. The functional importance of one of these conserved regions was shown by mutagenesis. Disruption of MBR1 leads to a partial growth defect on glycerol medium. Disruption of MBR3 has no major effect but the double disruptant shows a synthetic phenotype suggesting that the MBR1 and MBR3 gene products participate in common function.
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    Identification of a sporulation-specific promoter regulating divergent transcription of two novel sporulation genes in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 661-672 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Meiosis Sporulation ; Divergent promoter ; Developmental regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Promoters that control gene expression in Saccharomyces cerevisiae only in a sporulation-specific manner have previously been isolated from a genomic yeast DNA library fused to a promoterless Escherichia coli lacZ gene. Two novel sporulation-specific genes, SPS18 and SPS19, were isolated using this technique. These genes are divergently controlled by the same promoter but with SPS18 expressed at four times the level of SPS19. Deletion analysis has shown that the promoter elements that exert sporulation control on each of the genes overlap, having a common 25 bp sequence located within the intergenic region. SPS18 encodes a 34-KDa protein of 300 amino acids that contains a putative zinc-binding domain and a region of highly basic residues that could target the protein to the nucleus. SPS19 encodes a 31-KDa protein of 295 amino acids, which has a peroxisomal targeting signal (SKL) at its C terminus; this protein belongs to the family of non-metallo short-chain alcohol dehydrogenases. A null mutation deleting the intergenic promoter prevented expression of both genes, and when homozygous in diploids, reduced the extent of sporulation four-fold; the spores that did form were viable, but failed to become resistant to ether, and were more sensitive to lytic enzymes. This phenotype reflects a defect in spore wall maturation, indicating that the product of at least one of the genes functions during the process of spore wall formation. Therefore these genes belong to the class of late sporulation-specific genes that are sequentially activated during the process of meiosis and spore formation.
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    Use of synthetic lethal mutants to clone and characterize a novel CTP synthetase gene in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 431-439 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Duplicate genes ; Synthetic lethal mutants ; CTP synthetase ; Pyrimidine biosynthetic pathway
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In the pyrimidine biosynthetic pathway, CTP synthetase catalyses the conversion of uridine 5′-triphosphate (UTP) to cytidine 5′-triphosphate (CTP). In the yeast Saccharomyces cerevisiae, the URA7 gene encoding this enzyme was previously shown to be nonessential for cell viability. The present paper describes the selection of synthetic lethal mutants in the CTP biosynthetic pathway that led us to clone a second gene, named URA8, which also encodes a CTP synthetase. Comparison of the predicted amino acid sequences of the products of URA7 and URA8 shows 78% identity. Deletion of the URA8 gene is viable in a haploid strain but simultaneous presence of null alleles both URA7 and URA8 is lethal. Based on the codon bias values for the two genes and the intracellular concentrations of CTP in strains deleted for one of the two genes, relative to the wild-type level, URA7 appears to be the major gene for CTP biosynthesis. Nevertheless, URA8 alone also allows yeast growth, at least under standard laboratory conditions.
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    Temperature-sensitive mutants of hsp82 of the budding yeast Saccharomyces cerevisiae (1994)
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    Molecular genetics and genomics 242 (1994), S. 517-527 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; HSP82 ; Random in vitro mutagenesis ; Temperature-sensitive mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The budding yeast Saccharomyces cerevisiae has two HSP90-related genes per haploid genome, HSP82 and HSC82. Random mutations were induced in vitro in the HSP82 gene by treatment of the plasmid with hydroxylamine. Four temperature-sensitive (ts) mutants and one simultaneously is and cold-sensitivie (cs) mutant were then selected in a yeast strain in which HSC82 had previously been disrupted. The mutants were found to have single base changes in the coding region, which caused single amino acid substitutions in the HSP82 protein. All of these mutations occurred in amino acid residues that are well conserved among HSP90-related proteins of various species from Escherichia coli to human. Various properties including cell morphology, macromolecular syntheses and thermosensitivity were examined in each mutant at both the permissive and nonpermissive temperatures. The mutations in HSP82 caused pleiotropic effects on these properties although the phenotypes exhibited at the nonpermissive temperature varied among the mutants.
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    The hypo-osmolarity-sensitive phenotype of the Saccharomyces cerevisiae hpo2 mutant is due to a mutation in PKC1, which regulates expression of β-glucanase (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 641-648 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Cell wall ; Protein kinase C ; β-Glucanase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract To obtain more information about the cell wall organization of Saccharomyces cerevisiae, we have developed a novel screening system to obtain cell wall-defective mutants, using a density gradient centrifugation method. Nine hypo-osmolarity-sensitive mutants were classified into two complementation groups, hpo1 and hpo2. Phase contrast microscopic observation showed that mutant cells bearing lesions at either locus became abnormally large. A gene that complemented the mutant phenotype of hpo2 was cloned and sequenced. This gene turned out to be identical to PKC1, which encodes the yeast homologue of mammalian protein kinase C. Complementation tests with pkc1Δ showed that hpo2 is allelic to pkc1. To study the reason for the fragility of hpo2 cells, cell wall was isolated and the glucan was analyzed. The amount of alkali, acid-insoluble glucan, which is responsible for the rigidity of the cell wall, was reduced to about 30% that of the wild-type cell and this may be the major cause of the fragility of the hpo2 mutant cell. Analysis of total wall proteins in hpo2 mutant cells on SDS-polyacrylamide gels revealed that a 33 kDa protein was overproduced two- to threefold relative to the wild-type level. This 33 kDa protein was identified as a β-glucanase, encoded by BGL2. Disruption of BGL2 in the hpo2 mutant partially rescued the growth rate defect. This suggests that the PKC1 kinase cascade regulates BGL2 expression negatively and overproduction of the β-glucanase is partially responsible for the growth defect. Since the bgl2 disruption did not rescue the hypo-osmolarty-sensitive phenotype of the hpo2 mutant, PKC1 must negatively regulate other enzymes involved in the biosynthesis and metabolism of the cell wall.
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    Polyubiquitin gene expression contributes to oxidative stress resistance in respiratory yeast (Saccharomyces cerevisiae) (1994)
    Springer
    Molecular genetics and genomics 243 (1994), S. 358-362 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Oxidative stress ; High temperature viability ; Ubiquitin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract UBI4, the polyubiquitin gene of Saccharomyces cerevisiae, is expressed at a low level in vegetative cells, yet induced strongly in response to starvation, cadmium, DNA-damaging agents and heat shock. UBI4 is also expressed at a higher basal level in cells growing by respiration as compared to glucose-repressed cells growing by fermentation. This higher UBI4 expression of respiratory cultures probably helps to counteract the greater oxidative stress of respiratory growth. The effects of inactivating UBI4 on high temperature viability are more marked with respiratory cultures. Also loss of UBI4 leads to a considerably increased rate of killing of respiring cells by hydrogen peroxide, whereas the same gene inactivation has relatively little effect on the peroxide sensitivity of cells in which mitochondrial functions are repressed. This is the first study to reveal that ubiquitin levels in cells can influence their ability to withstand oxidative stress.
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    Open reading frames in the antisense strands of genes coding for glycolytic enzymes in Saccharomyces cerevisiae (1994)
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    Molecular genetics and genomics 243 (1994), S. 363-368 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Glycolysis ; Phosphoglucose isomerase ; Antisense ; Double-strand coding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Open reading frames longer than 300 bases were observed in the antisense strands of the genes coding for the glycolytic enzymes phosphoglucose isomerase, phosphoglycerate mutase, pyruvate kinase and alcohol dehydrogenase I. The open reading frames on both strands are in codon register. It has been suggested that proteins coded in codon register by complementary DNA strands can bind to each other. Consequently, it was interesting to investigate whether the open reading frames in the antisense strands of glycolytic enzyme genes are functional. We used oligonucleotide-directed mutagenesis of the PGI1 phosphoglucose isomerase gene to introduce pairs of closely spaced base substitutions that resulted in stop codons in one strand and only silent replacements in the other. Introduction of the two stop codons into the PGI1 sense strand caused the same physiological defects as already observed for pgi1 deletion mutants. No detectable effects were caused by the two stop codons in the antisense strand. A deletion that removed a section from − 31 by to + 109 by of the PGI1 gene but left 83 bases of the 3′ region beyond the antisense open reading frame had the same phenotype as a deletion removing both reading frames. A similar pair of deletions of the PYK1 gene and its antisense reading frame showed identical defects. Our own Northern experiments and those reported by other authors using double-stranded probes detected only one transcript for each gene. These observations indicate that the antisense reading frames are not functional. On the other hand, evidence is provided to show that the rather long reading frames in the antisense strands of these glycolytic enzyme genes could arise from the strongly selective codon usage in highly expressed yeast genes, which reduces the frequency of stop codons in the antisense strand.
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    The archaebacterial membrane protein bacterio-opsin is expressed and N-terminally processed in the yeast Saccharomyces cerevisiae (1994)
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    Molecular genetics and genomics 244 (1994), S. 183-188 
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    ISSN: 1617-4623
    Keywords: Bacterio-opsin ; Expression ; Yeast ; Saccharomyces cerevisiae ; Membranes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The bop gene codes for the membrane protein bacterio-opsin (BO), which on binding all-trans-retinal, constitutes the light-driven proton pump bacteriorhodopsin (BR) in the archaebacterium Halobacterium salinarium The designation H. salinarium instead of the former designation H. halobium is used throughout this paper following the classification of Tindall (1992) . This gene was cloned in a yeast multi-copy vector and expressed in Saccharomyces cerevisiae under the control of the constitutive ADH1 promoter. Both the authentic gene and a modified form lacking the precursor sequence were expressed in yeast. Both proteins are incorporated into the membrane in S. cerevisiae. The presequence is thus not required for membrane targeting and insertion of the archaebacterial protein in budding yeast, or in the fission yeast Schizosaccharomyces pombe, as has been shown previously. However, in contrast to S. pombe transformants, which take on a reddish colour when all-trans-retinal is added to the culture medium as a result of the in vivo regeneration of the pigment, S. cerevisiae cells expressing BO do not take on a red colour. The precursor of BO is processed to a protein identical in size to the mature BO found in the purple membrane of Halobacterium. The efficiency of processing in S. cerevisiae is dependent on growth phase, as well as on the composition of the medium and on the strain used. The efficiency of processing of BR is reduced in S. pombe and in a retinal-deficient strain of H. salinarium, when retinal is present in the medium.
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    Heterospecific cloning of Arabidopsis thaliana cDNAs by direct complementation of pyrimidine auxotrophic mutants of Saccharomyces cerevisiae. I. Cloning and sequence analysis of two cDNAs catalysing the second, fifth and sixth steps of the de novo pyrimidine biosynthesis pathway (1994)
    Springer
    Molecular genetics and genomics 244 (1994), S. 23-32 
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    ISSN: 1617-4623
    Keywords: Arabidopsis thaliana ; Saccharomyces cerevisiae ; Complementation ; Aspartate transcarbamylase ; Orotate phosphoribosyl transferase ; Orotidine-5′-phosphate decarboxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An Arabidopsis thaliana cDNA library was used to complement Saccharomyces cerevisiae pyrimidine auxotrophic mutants. Mutants in all but one (carbamylphosphate synthetase) of the six steps in the de novo pyrimidine biosynthetic pathway could be complemented. We report here the cloning, sequencing and computer analysis of two cDNAs encoding the aspartate transcarbamylase (ATCase; EC 2.1.3.2) and orotate phosphoribosyltransferase-orotidine-5′-phosphate decarboxylase (OPRTase-OMP-decase; EC 2.4.2.10, EC 4.1.1.23) enzymes. These results confirm the presence in A. thaliana of a bifunctional gene whose product catalyses the last two steps of the pyrimidine biosynthetic pathway, as previously suggested by biochemical studies. The ATCase encoding cDNA sequence (PYRB gene) shows an open reading frame (ORF) of 1173 by coding for 390 amino acids. The cDNA encoding OPRTase-OMPdecase (PYRE-F gene) shows an ORF of 1431 by coding for 476 amino acids. Computer analysis of the deduced amino acid sequences of both cDNAs shows the expected high similarity with the ATCase, ornithine transcarbamylase (OTCase; EC 2.1.3.3), OPRTase and OMPdecase families. This heterospecific cloning approach increases our understanding of the genetic organization and interspecific functional conservation of the pyrimidine biosynthetic pathway and underlines its usefulness as a model for evolutionary studies.
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    URL: http://dx.doi.org/10.1007/BF00280183
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    Sequence of the HAP3 transcription factor of Kluyveromyces lactis predicts the presence of a novel 4-cysteine zinc-finger motif (1994)
    Springer
    Molecular genetics and genomics 245 (1994), S. 96-106 
    Details
    ISSN: 1617-4623
    Keywords: HAP3 ; Saccharomyces cerevisiae ; Kluyveromyces lactis ; Zinc finger ; Carbon source regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Kluyveromyces lactis homologue of the Saccharomyces cerevisiae HAP3 gene was isolated by functional complementation of the respiratory-deficient phenotype of the S. cerevisiae hap3::HIS4 strain SHY40. The KlHAP3 gene encodes a protein of 205 amino acids, of which the central B-domain of 90 residues is highly homologous to HAP3 counterparts of S. cerevisiae and higher eukaryotes. The protein contains a novel 4-cysteine zinc-finger motif and we propose by analogy that all other homologous HAP3 proteins contain the same motif, with the position containing the third cysteine being occupied by a serine residue. In contrast to the situation in S. cerevisiae, disruption of the KlHAP3 gene in K. lactis does not result in a respiratory-deficient phenotype and the growth of the null strain is indistinguishable from wild type. There is also no effect on the expression of the carbon source-regulated KlCYC1 gene, suggesting either a different role for the HAP2/3/4 complex, or the existence of a different mechanism of carbon source regulation. Sequence verification of the S. cerevisiae HAP3 locus reveals that, just as in K. lactis, a long open reading frame (ORF) is present upstream of the HAP3 gene. These highly homologous ORFs are predicted to have at least eight membrane-spanning fragments, but do not show significant homology to any known sequence present in databases. The ScORFX gene is transcribed in the opposite direction to ScHAP3, but, in contrast to an earlier report by Hahn et al. (1988), the transcripts of the two genes do not overlap. The model proposed by these authors, in which the ScHAP3 gene is regulated by an anti-sense non-coding mRNA, is therefore not correct.
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    Expression of human poly(ADP-ribose) polymerase in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 245 (1994), S. 686-693 
    Details
    ISSN: 1617-4623
    Keywords: Yeast ; Saccharomyces cerevisiae ; Poly(ADP-ribose) polymerase ; DNA repair
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The coding sequence for human poly(ADP-ribose) polymerase was expressed inducibly in Saccharomyces cerevisiae from a low-copy-number plasmid vector. Cell free extracts of induced cells had poly(ADPribose) polymerase activity when assayed under standard conditions; activity could not be detected in non-induced cell extracts. Induced cells formed poly(ADP-ribose) in vivo, and levels of these polymers increased when cells were treated with the alkylating agent N-methyl-N′-nitro-N-nitrosoguanidine (MNNG). The cytotoxicity of this agent was increased in induced cells, and in vivo labelling with [3H]adenine further decreased their viability. Increased levels of poly(ADP-ribose) found in cells treated with the alkylating agent were not accompanied by lowering of the NAD concentration.
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    A new yeast gene, HTR1, required for growth at high temperature, is needed for recovery from mating pheromone-induced G1 arrest (1994)
    Springer
    Molecular genetics and genomics 245 (1994), S. 107-116 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; ts mutant ; Recovery ; HTR1 ; MCS1/SSD1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A new temperature-sensitive mutant of Saccharomyces cerevisiae was isolated. Arrested cells grown at the nonpermissive temperature were of dumb-bell shape and contained large vacuoles. A DNA fragment was cloned based on its ability to complement this temperature sensitivity. The HTR1 gene encodes a putative protein of 93 kDa without significant homology to any known proteins. The gene was mapped between ade5 and lys5 on the left arm of chromosome VII. The phenotype of the gene disruptant appeared to be strain-specific; disruption of the gene in strain W303 caused the cells to become temperature sensitive. The arrested phenotype here was similar to that of the original is mutant and cells in G2/M phase predominated at high temperature. Another disruptant in a strain YPH background grew slowly at high temperature due to slow progression through G2/M phase, and morphologically abnormal (elongated) cells accumulated. A single-copy suppressor that alleviated the temperature-sensitive defects in both strains was identified as MCS1/SSD1. The wild-type strains W303 and YPH are known to carry defective MCS1/SSD1 alleles; hence HTR1 may function redundantly with MCS1/SSD1 to suppress the temperature-sensitive phenotypes. In addition, based on a halo bioassay, the disruptant strains appeared to be defective in recovery from, or adaptive response to G1 arrest mediated by mating pheromone, even at the permissive temperature. Thus the gene has at least two functions and is designated HTR1 (required for high temperature growth and recovery from G1 arrest induced by mating pheromone).
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    Two subclasses of guanine exchange factor (GEF) domains revealed by comparison of activities of chimeric genes constructed from CDC25, SDC25 and BUD5 in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 245 (1994), S. 167-176 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Cell cycle ; Bud site selection ; Guanine exchange factor ; Ras
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Guanine Exchange Factor (GEF) activity for Ras proteins has been associated with a conserved domain in Cdc25p, Sdc25p in Saccharomyces cerevisiae and several other proteins recently found in other eukaryotes. We have assessed the structure-function relationships between three different members of this family in S. cerevisiae, Cdc25p, Sdc25p and Bud5p. Cdc25p controls the Ras pathway, whereas Bud5p controls bud site localization. We demonstrate that the GEF domain of Sdc25p is closely related to that of Cdc25p. We first constructed a thermosensitive allele of SDC25 by specifically altering amino acid positions known to be changed in the cdc25-1 mutation. Secondly, we constructed three chimeric genes from CDC25 and SDC25, the products of which are as active in the Ras pathway as are the wild-type proteins. In contrast, similar chimeras made between CDC25 and BUD5 lead to proteins that are inactive both in the Ras and budding control pathways. This difference in the ability of chimeric proteins to retain activity allows us to define two subclasses of structurally different GEFs: Cdc25p and Sdc25p are Ras-specific GEFs, and Bud5p is a putative GEF for the Rsr1/Bud1 Rap-like protein.
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    Inactivation of SSM4, a new Saccharomyces cerevisiae gene, suppresses mRNA instability due to rna14 mutations (1994)
    Springer
    Molecular genetics and genomics 245 (1994), S. 323-333 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; mRNA decay Poly(A) tail ; Ty transposition ; SSM4 gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Decay rates of mRNAs depend on many elements and among these, the role of the poly(A) tail is now well established. In the yeast Saccharomyces cerevisiae, thermosensitive mutations in two genes, RNA14 and RNA15, result in mRNAs having shorter poly(A) tails and reduced half-life. To identify other components interacting in the same process, we have used a genetic approach to isolate mutations that suppress the thermosensitivity of an rna14 mutant strain. Mutations in a single locus, named SSM4, not only suppress the cell growth phenotype but also the mRNA instability and extend the short mRNA poly(A) tails. The frequency of appearance and the recessive nature of these mutations suggested that the suppressor effect was probably due to a loss of function. We failed to clone the SSM4 gene directly by complementation, owing to its absence from gene banks; it later emerged that the gene is toxic to Escherichia coli, but we have nevertheless been able to clone the SSM4 sequence by Ty element transposition tagging. Disruption of the SSM4 gene does not affect cell viability and suppresses the rna14 mutant phenotypes. The protein encoded by the SSM4 gene has a calculated molecular mass of 151 kDa and does not contain any known motif or show homology with known proteins. The toxicity of the SSM4 gene in E. coli suggests that a direct biochemical activity is associated with the corresponding protein.
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    Genetic interaction between the Ras-CAMP pathway and the Dis2s1/Glc7 protein phosphatase in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 257-262 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Protein phosphatase ; Ras-cAMP pathway ; DIS2S1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Saccharomyces cerevisiae DIS2S1/GLC7 gene encodes a type 1 protein phosphatase indispensable for cell proliferation. We found that introduction of a multicopy DIS2S1 plasmid impaired growth of cells with reduced activity of the cAMP-dependent protein kinase. In order to understand further the interaction between the two enzymes, a temperature-sensitive mutation in the DIS2S1 gene was isolated. The mutant accumulated less glycogen than wild type at the permissive temperature, indicating that activity of the Dis2s1 protein phosphatase is attenuated by the mutation. Furthermore, the dis2s1 ts mutation was shown to be suppressed by a multicopy plasmid harboring PDE2, a gene for cAMP phosphodiesterase. These results indicate that the Ras-cAMP pathway interacts genetically with the DIS2S1/GLC7 gene.
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    Stress-induced transcriptional activation mediated by YAP1 and YAP2 genes that encode the Jun family of transcriptional activators in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 250-256 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Transcriptional activator ; AP-1 ; Stress response
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Saccharomyces cerevisiae YAP2 gene encoding an AP-1-like transcriptional activator protein was cloned by selection for genes that confer pleiotropic drug resistance when present in high copy number. The novel YAP2 gene encodes a protein of 45827 daltons and is homologous in part to a known transcriptional activator protein encoded by YAP1/PDR4/SNQ3/PAR1. Homology was found only in both terminal regions. The N-terminal portion contains a region rich in basic amino acids, followed by a “leucine zipper” motif. Overexpression of YAP2 led to the induction of expression of an AP-1 recognition element (ARE)-dependent promoter. The yap1 disruptant has been shown to be sensitive to H2O2. In this study, we demonstrated that the yap1 disruptant is also unable to grow in medium containing 150 μM cadmium, whereas the yap2 disruptant exhibited no significant phenotypes. However, YAP2 in high copy number did suppress cadmium sensitivity, but not H2O2 sensitivity of the yap1 disruptant. YAP1 was able to mediate both cadmium- and H2O2-induced transcriptional activation of an ARE-dependent promoter. A high-copy-number plasmid bearing YAP2 mediated cadmium-induced transcriptional activation of this promoter. The inductions were prevented by the antioxidant N-acetyl-l-cysteine.
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    The 3′ → 5′ exonucleases of both DNA polymerases δ and ε participate in correcting errors of DNA replication in Saccharomyces cerevisiae (1994)
    Springer
    Molecular genetics and genomics 242 (1994), S. 289-296 
    Details
    ISSN: 1617-4623
    Keywords: DNA polymerases ε and δ ; 3′ → 5′ Exonuclease ; Replication errors ; Spontaneous mutations ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract DNA polymerases II (ε) and III(δ) are the only nuclear DNA polymerases known to possess an intrinsic 3′ → 5′ exonuclease in Saccharomyces cerevisiae. We have investigated the spontaneous mutator phenotypes of DNA polymerase δ and ε 3′ → 5′ exonuclease-deficient mutants, pol3-01 and pol2-4, respectively. pol3-01 and pol2-4 increased spontaneous mutation rates by factors of the order of 102 and 101, respectively, measured as URA3 forward mutation and his7-2 reversion. Surprisingly, a double mutant pol2-4 pol3-01 haploid was inviable. This was probably due to accumulation of unedited errors, since a pol2-4/pol2-4 pol3-01/pol3-01 diploid was viable, with the spontaneous his7-2 reversion rate increased by about 2 × 103-fold. Analysis of mutation rates of double mutants indicated that the 3′ → 5′ exonucleases of DNA polymerases δ and ε can act competitively and that, like the 3′ → 5′ exonuclease of DNA polymerase δ the 3′ → 5′ exonuclease of DNA polymerase ε acts in series with the PMS1 mismatch correction system. Mutational spectra at a URA3 gene placed in both orientations near to a defined replication origin provided evidence that the 3′ → 5′ exonucleases of DNA polymerases δ and ε act on opposite DNA strands, but were in sufficient to distinguish conclusively between different models of DNA replication.
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    A novel method for efficient expression cloning of fungal enzyme genes (1994)
    Springer
    Molecular genetics and genomics 243 (1994), S. 253-260 
    Details
    ISSN: 1617-4623
    Keywords: Recombinant DNA ; Saccharomyces cerevisiae ; Endo-β-glucanase ; Endo-xylanase ; Heterologous expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have developed a method for fast and efficient isolation of enzyme genes from filamentous fungi by combining the ability of Saccharomyces cerevisiae to express heterologous genes with the utilisation of sensitive and reliable enzyme assays. A cDNA library from the fungus Humicola insolens was constructed in a S. cerevisiae/Escherichia coli shuttle vector in E. coli. Sub-pools of the library were subsequently screened for enzyme activity in S. cerevisiae. More than 130 clones were identified as positive in either an endo-β-glucanase or an endo-xylanase assay. Based on a partial characterization of the DNA sequence of the individual clones, they could be grouped into five distinct types of endo-β-glucanases and three types of endo-xylanases. A representative cDNA from each type was sub-cloned in an Aspergillus vector and expressed in A. oryzae. The new cloning method may be an important alternative to traditional cloning methods based on amino acid sequence information.
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    Efficient UV stimulation of yeast integrative transformation requires damage on both plasmid strands (1994)
    Springer
    Molecular genetics and genomics 243 (1994), S. 308-314 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Integrative plasmids ; Recombinational structures ; UV irradiation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The nature of UV-induced pre-recombinational structures was studied using transformation of Saccharomyces cerevisiae cells with non-replicative plasmids. Transformation by double-stranded plasmids irradiated with UV was stimulated up to 50-fold, and both plasmid integration and conversion of the mutated chromosomal selective gene were found to be equally increased. The stimulation observed with such ‘totally’ irradiated plasmids was not found with plasmids bearing lesions in only one strand. This effect is attributed to the formation by excision repair of recombinogenic structures consisting of a pyrimidine dimer opposite a gap. When single-stranded integrative plasmids were irradiated, their transforming potential was decreased but the proportion of transformants that arose by gene conversion, rather than by plasmid integration, was increased from 8% to 49% as a function of the UV dose. Possible reasons why single-strand UV lesions favour gene conversion are discussed.
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    Shared control of maltose induction and catabolite repression of the MAL structural genes in Saccharomyces (1994)
    Springer
    Molecular genetics and genomics 243 (1994), S. 622-630 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Yeast Catabolite repression ; Gene expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Maltose utilization in yeast requires the presence of any one of the five unlinked, homologous MAL loci. Transcription of the two structural genes MALT (permease) and MALS (maltase) is induced by maltose and catabolite-repressed by glucose. MAL6T and MAL6S share a common 5′ intergenic sequence; deletion studies within this sequence revealed a bi-directionally functioning upstream activation sequence (UASM) consisting of four 11bp homologous sites. Activation of these sites by the MALR protein results in the coordinate expression of MAL6T and MAL6S. The basal promoter activates MALS expression to a greater extent than MALT and is located in a region that overlaps UASM. Deletion of several subsites within the UASM has an asymmetric effect on MAL gene expression, having a greater affect on MALT than on MALS. Catabolite repression of MAL6T and MAL6S by glucose is controlled at several levels. Using disruption mutants, the positively acting MAL1R protein was also found to play a role in catabolite repression of MAL6T and MAL6S.
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    RPK1, an essential yeast protein kinase involved in the regulation of the onset of mitosis, shows homology to mammalian dual-specificity kinases (1994)
    Springer
    Molecular genetics and genomics 243 (1994), S. 641-653 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; RPK1 gene ; Protein kinase ; DNA replication ; Initiation of mitosis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We report here the sequence of RPK1 (for Regulatory cell Proliferation Kinase), a new Saccharomyces cerevisiae gene coding for a protein with sequence similarities to serine/threonine protein kinases. The protein sequence of 764 amino acids includes an amino-terminal domain (residues 1–410), which may be involved in regulation of the kinase domain (residues 411–764). The catalytic domain of Rpkl is not closely related to other known yeast protein kinases but exhibits strong homology to a newly discovered group of mammalian kinases (PYT, TTK, esk) with serine/threonine/tyrosine kinase activity. Null alleles of RPK1 are lethal and thus this gene belongs to the small group of yeast protein kinase genes that are essential for cell growth. In addition, eliminating the expression of RPK1 gives rise to the accumulation of non-viable cells with less than a 1 N DNA content suggesting that cells proceed into mitosis without completion of DNA synthesis. Therefore, the Rpkt kinase may function in a checkpoint control which couples DNA replication to mitosis. The level of the RPK1 transcript is extremely low and constant throughout the mitotic cycle. However it is regulated during cellular differentiation, being decreased in α-factor-treated a cells and increased late in meiosis in a/α diploids. Taken together, our results suggest that Rpk1 is involved in a pathway that coordinates cell proliferation and differentiation.
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    Lysine inhibition of Saccharomyces cerevisiae: role of repressible L-lysine ε-aminotransferase (1994)
    Springer
    World journal of microbiology and biotechnology 10 (1994), S. 572-575 
    Details
    ISSN: 1573-0972
    Keywords: Growth inhibition ; L-lysine ε-aminotransferase ; nitrogen limitation ; α-oxoadipic acid ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Lysine added to grain mashes under nitrogen-limiting conditions (as in most industrial fermentations) inhibited growth of Saccharomyces cerevisiae. This inhibition was relieved by raising the assimilable nitrogen content. Lysine-induced inhibition is not mediated through accumulation of α-oxoadipic acid, an intermediate of lysine metabolism which accumulates by a back up of intermediates in de novo synthesis. Lysine degradation is regulated by the synthesis of L-lysine ε-aminotransferase, an enzyme that catalyses the first step in one of three possible routes of lysine degradation (not previously reported in S. cerevisiae). Synthesis is repressed under nitrogenlimiting conditions, but derepressed when excess assimilable nitrogen is available. Derepression results in degradation of lysine and decreases inhibitory effects on growth. The toxic compound appears to be lysine itself.
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    Crossflow filtration of yeast broth cultivated in molasses (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 43 (1994), S. 1094-1101 
    Details
    ISSN: 0006-3592
    Keywords: crossflow filtration ; microfiltration ; Saccharomyces cerevisiae ; molasses ; backwashing ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A broth of yeast cells cultivated in molasses was crossfiltered with a thin-channel module. The permeation flux gradually decreased at a constant cell concentration. The flux was much lower than that obtained for yeast broth cultivated in yeast extract, polypeptone, and dextrose (YPD) medium during the filtration. The flux did not depend on the membrane pore size (0.45 to 5 μm). The steady-state flux was one-twentieth that calculated for a cake filtration mode from the amount of cake per unit filtration area and the specific resistance of the cake measured in a dead-end filtration apparatus. The lower flux was due to small particles (most of which were less than 1 μm in diameter) in the molasses. The mehanism of crossflow filtration of broths of yeast cells cultivated in molasses was clarified by analysis of the change in flux with time and observations with scanning electron microscopy. At the initial stage of crossflow filtration the yeast cells and particles from the molasses were deposited on the membrane to form the molasses were deposited on the membrane to form a cake in a similar way to dead-end filtration. After the deposition of cells onto the membrane ceased, the fine particles from molasses formed a thin layer, which had higher resistance than the cake formed next to the membrane. The backwashing method was effective to increase the flux. The flux increased low when the pore size was 0.45 to 0.08 μm, but using larger pores of 3 to 5 μm it returned almost to the bases line. © 1994 John Wiley & Sons, Inc.
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    Ethanol production from nonsterilized carob pod extract by free and immobilized Saccharomyces cerevisiae cells using fed-batch culture (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 43 (1994), S. 189-194 
    Details
    ISSN: 0006-3592
    Keywords: ethanol ; Saccharomyces cerevisiae ; carob pod ; fed-batch culture ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The production of ethanol from carob pod extract by free and immobilized Saccharomyces cerevisiae cells in batch and fed-batch culture was investigated. Fed-batch culture proved to be a better fermentation system for the production of ethanol than batch culture. In fed-batch culture, both free and immobilized S. cerevisiae cells gave the same maximum concentration (62 g/L) of final ethanol at an initial sugar concentration of 300 g/L and F = 167 mL/h. The maximum ethanol productivity (4.4 g/L h) was obtained with both free and immobilized cells at a substrate concentration of 300 g/L and F = 334 mL/h. In repeated fed-batch culture, immobilized S. cerevisiae cells gave a higher overall ethanol concentration compared with the free cells. The immobilized S. cerevisiae cells in Ca-alginate beads retained their ability to produce ethanol for 10 days. © 1994 John Wiley & Sons, Inc.
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    Physicochemical properties of the matrix proteins of three main culture vehicles (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 44 (1994), S. 29-37 
    Details
    ISSN: 0006-3592
    Keywords: proteins, contaminant ; Escherichia coli ; Saccharomyces cerevisiae ; mammalian cell culture ; PAGE ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The protein components of three industrial recombinant expression systems: Escherichia coli, Saccharomyces cerevisiae, and a mammalian cell culture supernatant of CHO cells were characterized in terms of their molecular weight, isoelectric point, and relative surface hydrophobicity. Identification of individual proteins was done by reference to their position in protein band profiles by polyacrylamide gel electrophoresis (PAGE) of the crude material. This permitted a rapid and facile assignment of quantitative values for these three parameters to all the major protein components in these materials. Because it is the indigenous proteins in expression systems that will form the bulk of any impurities in the product, once the values of these parameters are known for any target recombinant protein, the data obtained will enable appropriate expression systems to be chosen for minimizing amounts of potential contaminants and reducing downstream processing requirements and costs. The data will also indicate which fractionation steps (i.e., charge, size or hydrophobicity-based) are likely to be best for distinguishing between target and contaminant proteins, thus aiding and early removal of the maximum quantities of undesired protein to bring subsequent bioseparation steps down in scale and cost and up in terms of efficiency. © 1994 John Wiley & Sons, Inc.
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    Real and pseudo oxygen gradients in Ca-alginate beads monitored during polarographic Po2-measurements using Pt-needle microelectrodes (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 44 (1994), S. 617-625 
    Details
    ISSN: 0006-3592
    Keywords: oxygen profiles ; oxygen microprobe ; Po2-microelectrode ; artifacts ; alginate beads ; Saccharomyces cerevisiae ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Polarographic microcoaxial needle electrodes were used to measure internal profiles of dissolved oxygen tension (Po2) within single Ca-alginate beads of different diameter containing entrapped cells of Saccharomyces cerevisiae. For the investigations, single beads coming from variable growing conditions and distinct cultivation stages were fixed in a special holding device. In dependence on microbial growth steep oxygen gradients were observed. The Oxygen penetration depth at steady state lay between 50 and 100 μm. After 8 h of cultivation time, the anaerobic space within the beads (φ 2 mm; cultivation in a packed bed reactor) is beginning at ∼ 130 μm, whereas the anaerobic space within the beads (φ 2 mm) coming from the shaker flask culture is located ∼440 μm below the bead surface. Surprisingly, steep gradients were also observed, when recording profiles from cell-free Ca-alginate beads of different diameter and alginate concentrations. The steep oxygen gradients apparently had to be interpreted as pseudo-Po2-gradients. These results were borne by several effects, such as formation of artifacts and diffusion barriers in front of the electrode tip or oxygen “availability” at the tip and consumption of oxygen by the electrode itself. These phenomena could be documented by microscopic observation and photography. Thus, to obtain real Po2-profiles it is important to be exactly informed about the physical, chemical, and biological properties of the material to be investigated. Furthermore, it is necessary to apply a special stepwise puncture technique with distinct step-in/step-out movements of the electrode: e.g., unidirectional or contradirectional puncture techniques. © 1994 John Wiley & Sons, Inc.
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    The use of hollow fiber cross-flow microfiltration in bioaccumulation and continuous removal of heavy metals from solution by Saccharomyces cerevisiae (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 44 (1994), S. 1362-1366 
    Details
    ISSN: 0006-3592
    Keywords: Saccharomyces cerevisiae ; bioaccumulation ; gel immobilization ; cross-flow microfiltration ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Cross-flow microfiltration was shown to retain Saccharomyces cerevisiae biomass utilized for heavy metal bioaccumulation. The passage of metal-laden influent through a series of sequential bioaccumulation systems allowed for further reductions in the levels of copper, cadmium, and cobalt in the final effluent than that afforded by a single bioaccumulation process. Serial bioaccumulation systems also allowed for partial separation of metals from dual metal influents. More than one elemental metal cation could be accumulated simultaneously and in greater quantities than when a single metal was present in the effluent (Cu2+ 0.43 mmol, Cu2+ + Cd2+ 0.67 mmol, and Cu2+ + Co2+ 0.83 mmol/g yeast dry mass when the initial concentration of each of the metal species was 0.2 mmol·L-1). Co-accumulation of two different metal cations allowed higher total levels of bioaccumulation than found with a single metal. The flux rate was 2.9 × 102 L·h-2μm-2 using a polypropylene microfiltration membrane (0.1 μm pore size) at 25°C. © 1994 John Wiley & Sons, Inc.
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    The release of virus-like particles from recombinant Saccharomyces cerevisiae: Effect of freezing and thawing on homogenization and bead milling (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 44 (1994), S. 736-744 
    Details
    ISSN: 0006-3592
    Keywords: disruption kinetics ; Saccharomyces cerevisiae ; virus-like particles ; recombinant cells ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Recombinant cells of Saccharomyces cerevisiae, expressing virus-like particles (Ty-VLPs), can be readily disrupted in a high pressure homogenizer and show identical disruption kinetics to the untransformed host strain. When the cells are freeze/thawed before disruption, they become about four times more resistant to homogenization. This effect increases with the number of freeze/thaw cycles, but is independent of the time the cells remain frozen. The freeze/thaw effect is observed with cells harvested during both the logarithmic and stationary phase of growth, and occurs with the untransformed host strain as well as the transformed one. Freeze/thawed cells are twice as resistant to disruption in the bead mill as fresh cells. © 1994 John Wiley & Sons, Inc.
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    Increased thermostability of Asn182 → Ala mutant Aspergillus awamori glucoamylase (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 43 (1994), S. 101-105 
    Details
    ISSN: 0006-3592
    Keywords: Aspergillus awamori ; glucoamylase ; kinetic ; thermostability ; Saccharomyces cerevisiae ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Asn182 → Ala Aspergillus awamori glucoamylase expressed in Saccharomyces cerevisiae had a first-order thermodeactivation coefficient 40% that of wild-type glucoamylase at pH 4.5 between 60° and 65°C, caused by the elimination of an Asn - Gly sequence subject to deamidation and eventual chain breakage. Above 70°C, and at pHs 3.5 and 5.5, thermodeactivation coefficients of wild-type and mutant enzymes were roughly equal, because the fastest deactivation mechanism was no longer deamidation. The mutation had little effect on the enzyme's optimal pH for activity and subsite map, or on the glucose yield from starch dextrin hydrolysis. During enzyme production by yeast fermentation, highest cell densities and activities of wild-type and mutant glucoamylases were attained after a period of glucose starvation, followed by a second addition of glucose. © 1994 John Wiley & Sons, Inc.
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    Diffusion of acetophenone and phenethyl alcohol in the calcium-alginate-bakers' yeast-hexane system (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 44 (1994), S. 1217-1227 
    Details
    ISSN: 0006-3592
    Keywords: acetophenone ; phenethyl alcohol ; Saccharomyces cerevisiae ; diffusion coefficient ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The intrabead diffusion coefficients of acetophenone and phenethyl alcohol were measured at 30°C in the triphasic immobilized yeast-water-hexane system. Saccharomyces cerevisiae cells were deactivated with hydrochloric acid and entrapped in calcium-alginate beads. Measurements of dry cell loss during deactivation, shrinkage of the beads during deactivation and the final porosity of the beads were made for various cell loadings. Final concentrations of wet cells in the beads ranged from approximately 0.25 to 0.30 g/mL. Mass transfer in the hexane phase, external to the beads, was eliminated experimentally. The estimated error of 5% to 10% in the diffusion coefficients is within the experimental error associated with the bead method. The effect of significant sampling volumes on the diffusivities was estimated theoretically and accounted for experimentally. The intrabead concentration of acetophenone and phenethyl alcohol was 150 to 800 ppm. The deactivated cells were shown to be impervious to acetophenone so that the measured diffusivities are extracellular parameters. The cell volume fraction in the beads ranged from 0.70 to 0.90, significantly higher than previously reported data. The effective diffusion coefficients conform to the random pore model. No diffusional interaction between acetophenone and phenethyl alcohol was observed. The addition of 2 vol% ethanol or methanol slightly increased the diffusivities. The thermodynamic partition coefficients were measured in the bead-free water-organic system and found to be an order of magnitude lower than the values calculated from the analysis of the diffusion data for the organic-bead system, suggesting that bead-free equilibrium data cannot be used in triphasic systems. © 1994 John Wiley & Sons, Inc.
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    Immobilization of “Disguised” yeast in chemically crosslinked chitosan beads (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 44 (1994), S. 1083-1088 
    Details
    ISSN: 0006-3592
    Keywords: chitosan ; crosslinking ; yeast immobilization ; Saccharomyces cerevisiae ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A new simple method for the preparation of chemically crosslinked chitosan beads is presented. It consists of the dropwise addition of 2-3% (w/v) low molecular weight chitosan solution containing 2% (w/v) glyoxal in 1% (w/v) tetrasodiumdiphosphate, pH 8.0. Immobilized viable baker's yeast (Saccharomyces cerevisiae) could be obtained via gel entrapment within the new beads when means preventing their direct contact with soluble chitosan were provided, “disguising” the cells until gelation and crosslinking were completed. Such means included cell suspension in castor oil or mixing with carboxymethyl-cellulose powder. Application of these means was shown to be necessary, as cells exposed to soluble chitosan immediately lost their viability and glycolytic activity. Yeast disguised in castor oil was also protected from bead reinforcement by glutaraldehyde treatment, significantly strengthening bead stability while operating under acidic conditions. This capability was demonstrated by continuous ethanol production by chitosan entrapped yeast. © 1994 John Wiley & Sons, Inc.
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    Molecular characterization of the SPT23 gene: A dosage-dependent suppressor of ty-induced promoter mutations from Saccharomyces cerevisiae (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 81-92 
    Details
    ISSN: 0749-503X
    Keywords: Retrotransposon ; transcription ; Saccharomyces cerevisiae ; chromosome XI ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: SPT genes are suppressors of mutations induced by the retrotransposon Ty in Saccharomyces cerevisiae. All SPT genes isolated to date suppress Ty-induced mutations by altering transcription. SPT23 was identified as a multicopy suppressor of the Ty-induced promoter mutations his4-912δ and lys2-61. Multicopy expression of SPT23 suppresses a variety of Ty-induced promoter mutations, including the MAT-regulated alleles his4-917 (480) and lys2-173R2. Here, we report the initial characterization of the SPT23 gene, including its nucleotide sequence and location in the yeast genome. The SPT23 gene contains a 1854 base pair open reading frame. Searches of the current data bases show no homology between SPT23 and previously described genes or proteins. The SPT23 gene is located between RAM2 and MAK11 on the left arm of chromosome XI. Tn10-LUK insertional mutagenesis of the SPT23 gene indicates that SPT23 is not essential for vegetative growth and spt23 mutations do not confer an Spt- phenotype.
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    URL: http://dx.doi.org/10.1002/yea.320100108
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    XI. Yeast sequencing reports. Analysis of an 11·7 kb DNA fragment of chromosome XI reveals a new tRNA gene and four new open reading frames including a leucine zipper protein and a homologue to the yeast mitochondrial regulator ABF2 (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 125-130 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome XI ; DNA-binding ; leucine zipper ; HMG box ; tRNAval. ; Kazal serine protease inhibitor signature ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We report the nucleotide sequence of an 11·7 kb fragment from the left arm of Saccharomyces cerevisiae chromosome XI. Analysis reveals a new tRNA for valine and four unknown open reading frames among which YKL245 shows homology with a yeast mitochondrial regulatory protein and YKL244, YKL246 and YKL247 are unknown.
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    URL: http://dx.doi.org/10.1002/yea.320100112
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    VI. Yeast sequencing reports. The sequence and potential regulatory elements of the HEM2 promoter of Saccharomyces cerevisiae (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 227-229 
    Details
    ISSN: 0749-503X
    Keywords: HEM2 ; promoter ; δ-aminolaevulinate dehydratase ; PBG synthetase ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: This paper reports the 1890-bp sequence located upstream of the HEM2 gene of Saccharomyces cerevisiae. The following potential regulatory protein-binding motifs were found: ABF1-binding site, yAP1-binding site, two REB1-binding sites, a cyclic AMP-responsive element, RAP1-binding site, and several HAP2-HAP3-HAP4 binding sites, implicating a complex regulatory mechanism governing expression for the HEM2 gene.
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    URL: http://dx.doi.org/10.1002/yea.320100209
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    XI. Yeast sequencing reports. Sequence analysis of a 3·5 kb EcoRI fragment from the left arm of Saccharomyces cerevisiae chromosome XI reveals the location of the MBR1 gene and a sequence related to a GTPase-activating protein (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 257-264 
    Details
    ISSN: 0749-503X
    Keywords: Genome sequencing ; Saccharomyces cerevisiae ; chromosome XI ; MBR1 ; GTPase-activating protein ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We present the DNA sequence analysis of a region covering a 3·5 kb EcoRI fragment from the left arm of chromosome XI from Saccharomyces cerevisiae. This region contains five open reading frames (ORFs) which code for proteins of greater than 100 amino acids. ORF YKL425 codes for the previously sequenced Mbr1 (Valens et al., 1991; Daignan-Fornier et al., 1993) which participates in mitochondrial biogenesis. YKL424 has identity with a GTPase-activating protein of higher eukaryotes. The three remaining ORFs have no identity to known proteins within the databases screened and are not assigned ORF numbers as they are completely contained with ORFs YKL424 and YKL425. This sequence has been entered in the EMBL Data Library under Accession Number X75561.
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    Multipurpose vectors designed for the fast generation of N- or C-terminal epitope-tagged proteins (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 105-112 
    Details
    ISSN: 0749-503X
    Keywords: Cloning vectors ; Saccharomyces cerevisiae ; fusion proteins ; epitope tagging ; immunodetection ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In this paper are described a set of new high-copy-number yeast vectors, which are specially designed for the conditional expression of epitope-tagged proteins in vivo. One of the major advantages of these plasmids is that they allow polymerase chain reaction-amplified open reading frames to be automatically fused in frame with the epitope-coding sequence, avoiding longer procedures such as site-directed mutagenesis. This heterologous construction can be realized either at the 5′-end of the coding sequence, in the pYeF1 vector, or at its 3′-end, in pYeF2, generating N- or C-terminal tagged proteins, respectively. Moreover, to increase the usefulness of the method, derivatives of the two basic URA3-borne pYeF1 and pYeF2 were constructed, carrying either the HIS3 or TRP1 gene as a marker of selection. These vectors could be of use for the purpose of functional analysis of the newly discovered genes resulting from the systematic sequencing of the yeast genome. Here, we present results showing the functional expression and the efficient immunoprecipitation of the epitope-tagged Rna15 protein, which is involved in Saccharomyces cerevisiae mRNA stability.
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    XI. Yeast sequencing reports. Sequence analysis of a 10 kb fragment of yeast chromosome XI identifies the SMY1 locus and reveals sequences related to a pre-mRNA splicing factor and vacuolar ATPase subunit C plus a number of unidentified open reading frames (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 247-255 
    Details
    ISSN: 0749-503X
    Keywords: Genome sequencing ; Saccharomyces cerevisiae ; chromosome XI ; SMY1 ; pre-mRNA splicing factor ; ATPase subunit C ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We report the DNA sequence analysis of a region on the left arm of chromosome XI of Saccharomyces cerevisiae extending over 10 kb. The region contains five open reading frames (ORFs) of greater than 100 amino acids which do not show significant overlap with other ORFs. YKL408 contains a sequence with strong similarity to the RNA helicase pre-mRNA splicing factors PRP2, PRP16 and PRP22 (Burgess et al., 1990; Company et al., 1991; Ruby et al., 1991). YKL409 corresponds to the gene SMY1, the sequence of which was previously reported by Lillie and Brown (1992). YKL410 is identical to ATPase subunit C (Beltran et al., 1992) except for an N-terminal extension. YKL406 and YKL407 show no significant identity with any sequences in the databases searched. The sequence has been entered in the EMBL Data Library under Accession Number X75560.
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    III. Yeast sequencing reports. Corrected sequence for the right telomere of Saccharomyces cerevisiae chromosome III (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 271-274 
    Details
    ISSN: 0749-503X
    Keywords: Genome sequencing ; Saccharomyces cerevisiae ; chromosome III ; telomeres ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A comparison of the sequences of telomere regions from several yeast chromosomes revealed an apparent cloning artifact for the right end of chromosome III. An integrating vector containing G1-3T telomere sequences was used to clone the right end of chromosome III from a strain related to S288C. The sequence of this clone confirmed that the published sequence was incorrect and demonstrated that the right telomere region of chromosome III is similar to other telomeres.
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    Sequence comparison of the ARG4 chromosomal regions from the two related yeasts, Saccharomyces cerevisiae and Saccharomyces douglasii (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 309-317 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; Saccharomyces douglasii ; evolution ; ARG4 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A 3·6 kb DNA fragment from Saccharomyces douglasii, containing the ARG4 gene, has been cloned, sequenced and compared to the corresponding region from Saccharomyces cerevisiae. The organization of this region is identical in both yeasts. It contains besides the ARG4 gene, another complete open reading frame (ORF) (YSD83) and a third incomplete one (DED81). The ARG4 and the YSD83 coding regions differ from their S. cerevisiae homologs by 8.1% and 12·5%, respectively, of base substitutions. The encoded proteins have evolved differently: amino acid replacements are significantly less frequent in Arg4 (2·8%) than in Ysc83 (12·4%) and most of the changes in Arg4 are conservative, which is not the case for Ysc83. The non-coding regions are less conserved, with small AT-rich insertions/deletions and 20% base substitutions. However, the level of divergence is smaller in the aligned sequences of these regions than in silent sites of the ORFs, probably revealing a higher degree of constraints. The Gcn4 binding site and the region where meiotic double-strand breaks occur, are fully conserved. The data confirm that these two yeasts are evolutionarily closely related and that comparisons of their sequences might reveal conserved protein and DNA domains not expected to be found in sequence comparisons between more diverged organisms.
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    XII. Yeast sequencing reports. Sequence, mapping and disruption of CCC1, a gene that cross-complements the Ca2+-sensitive phenotype of csg1 mutants (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 515-521 
    Details
    ISSN: 0749-503X
    Keywords: Ca2+ sensitive mutants ; cross-complementation ; Saccharomyces cerevisiae ; chromosome XII ; CCC1 ; calcium regulation ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have isolated, sequenced, mapped and disrupted a novel gene, CCC1, from Saccharomyces cerevisiae. This gene displays non-allelic complementation of the Ca2+-sensitive phenotype conferred by the csg1 mutation. The ability of this gene, in two copies per cell, to reverse the csg1 defect suggests it may have a role in regulating Ca2+ homeostasis. The sequence of CCC1 indicates that it encodes a 322 amino acid, membrane-associated protein. The CCC1 gene is located on the right arm of chromosome XII. The sequence has been deposited in the GenBank data library under Accession Number L24112.
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    VIII. Yeast mapping reports. Genetic mapping of STE20 to the left arm of chromosome VIII (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 693-695 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome VIII ; STE20 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: STE20 is a newly-discovered element of the Saccharomyces cerevisiae pheromone response pathway. We have isolated a recessive ste20 mutation and have used it to map the gene to the left arm of chromosome VIII, establishing the gene order STE20-CEN8-GPA1-ARG4.
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    A new nuclear suppressor system for a mitochondrial RNA polymerase mutant identifies an unusual zinc-finger protein and a polyglutamine domain protein in Saccharomyces cerevisiae (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 719-731 
    Details
    ISSN: 0749-503X
    Keywords: Transcription factors ; mitochondrial RNA polymerase ; zinc-finger protein ; glutamine domain ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A yeast strain with a point mutation in the nuclear gene for the core subunit of mitochondrial RNA polymerase was used to isolate new extragenic suppressors. Spontaneously occurring phenotypical revertants were analysed by crosses with the wild-type and tetrad dissection. One of the new nuclear suppressor mutants was characterized by temperature-sensitive growth on non-fermentable carbon sources. This mutant was transformed with a genomic yeast library. Two independent types of DNA clones were isolated which both complemented the temperature-sensitive defect. Subcloning and DNA sequencing identified two novel yeast genes which code for proteins with the characteristic features of transcription factors. Both factors exhibit highly structured protein domains consisting of runs and clusters of asparagine and glutamine residues. One of the proteins contains in addition zinc-finger domains of the C2H2-type. Therefore the genes are proposed to be named AZF1 (asparagine-rich zinc-ffinger protein) and PGD1 (polyglutamine domain protein). Gene disruption of both reading frames has no detectable influence on the vegetative growth on complete glucose or glycerol media, indicating that the genes may act as high copy number suppressors of the mutant defect. Additional transformation experiments showed that AZF1 is also an efficient suppressor for the original defect in the core subunit of mitochondrial RNA polymerase. The DNA sequences for the AZF1 and PGD1 genes were submitted to the EMBL data base (Accession Numbers: Z26253 and Z26254).
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    Defining the sequence specificity of the Saccharomyces cerevisiae DNA binding protein REB1p by selecting binding sites from random-sequence oligonucleotides (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 771-787 
    Details
    ISSN: 0749-503X
    Keywords: REB1 ; Saccharomyces cerevisiae ; random selection ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have used a random selection protocol to define the consensus and range of binding sites for the Saccharomyces cerevisiae REB1 protein. Thirty-five elements were sequenced which bound specifically to a GST-REB1p fusion protein coupled to glutathione-Sepharose under conditions in which more than 99·9% of the random sequences were not retained. Twenty-two of the elements contained the core sequence CGGGTRR, with all but one of the remaining elements containing only one deviation from the core. Of the core sequence, the only residues that were absolutely conserved were the three consecutive G residues. Statistical analysis of a nucleotide-use matrix suggested that the REB1p binding site also extends into flanking sequences with the optimal sequence for REB1p binding being GNGCCGGGGTAACNC. There was a positive correlation between the ability of the sites to bind in vitro and activate transcription in vivo; however, the presence of non-conformants suggests that the binding site may contribute more to transcriptional activation than simply allowing protein binding. Interestingly, one of the REB1p binding elements had a DNAse 1 footprint appreciably longer than other elements with similar affinity. Analysis of its sequence indicated the potential for a second REB1p binding site on the opposite strand. This suggests that two closely positioned low-affinity sites can function together as a highly active site. In addition, database searches with some of the randomly defined REB1p binding sites suggest that related elements are commonly found within ‘TATA-less’ promoters.
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    X. Yeast sequencing reports. Revised nucleotide sequence of the cor region of yeast Saccharomyces cerevisiae chromosome X (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 811-818 
    Details
    ISSN: 0749-503X
    Keywords: Yeast ; Saccharomyces cerevisiae ; chromosome X ; COR cluster ; genes CYC1 ; UTR1 ; UTR3 ; OSM1 ; tRNAGly ; RAD7 ; open reading frame: systematic sequencing ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The COR region, a gene cluster located on chromosome X of Saccharomyces cerevisiae and including genes CYC1, UTR1, UTR3, OSM1, tRNAGly and RAD7, was sequenced within the framework of the European Union genome systematic sequencing project. It was compared with previously published sequences to be found in GenBank under the acronym YSCCORA. While some of the discrepancies observed can be readily ascribed to polymorphism, others most probably result from sequencing errors. A revised version of the sequence of the COR cluster is given. The sequence has been deposited in the EMBL Data Library under Accession Number L26347.
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    IX. Yeast sequencing reports. Cloning and sequence of REV7, a gene whose function is required for DNA damage-induced mutagenesis in Saccharomyces cerevisiae (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 1503-1509 
    Details
    ISSN: 0749-503X
    Keywords: REV7 ; Saccharomyces cerevisiae ; induced mutagenesis ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The function of the REV7 gene is required for DNA damage-induced mutagenesis in budding yeast, Saccharomyces cerevisiae, and is therefore thought to promote replication past sites of mutagen damage in the DNA template. We have cloned this gene by complementation of the rev7-2 mutant defect, and determined its sequence. REV7 encodes a predicted protein of Mr 28 759 which is unlike any other protein in the NCBI non-redundant protein sequence data base, and which is inessential for viability. The sequence of the 3·88 kb yeast genomic fragment containing REV7 has been deposited in Genbank accession number U07228.
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    IIX. Yeast mapping reports. ATP1 and ATP2, the F1F0-ATPase α and β subunit genes of Saccharomyces cerevisiae, are respectively located on chromosomes II and X (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 1531-1534 
    Details
    ISSN: 0749-503X
    Keywords: F1F0-ATPase ; ATP1 ; ATP2 ; Saccharomyces cerevisiae ; chromosomes ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Southern blot analysis showed that ATP1 and ATP2 map on chromosomes II and X, respectively. Physical mapping of ATP1 and ATP2 by chromosome fragmentation showed that ATP1 is at the left end of chromosome II and ATP2 is at the right end of chromosome X. Both are located close to telomere sequences of each chromosome; ATP1 and ATP2 being approximately 30 kb and 85 kb from the respective telomeres.
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    Genome renewal: A new phenomenon revealed from a genetic study of 43 strains of Saccharomyces cerevisiae derived from natural fermentation of grape musts (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 1543-1552 
    Details
    ISSN: 0749-503X
    Keywords: Genome renewal ; wine yeast ; Saccharomyces cerevisiae ; homothallism ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have analyzed by genetic means 43 strains of Saccharomyces that had been isolated from fermenting grape musts in Italy. Twenty eight of these strains were isolated from 28 cellars in the Region of Emilia Romagna. The other 15 strains came from 5 fermentations at four cellars near the city of Arpino, which is located south and east of Rome.We found that 20 of the 28 strains from Emilia Romagna were heterozygous at from one to seven loci. The balance were, within the limits of our detection, completely homozygous. All these strains appeared to be diploid and most were homozygous for the homothallism gene (HO/HO). Spore viability varied greatly between the different strains and showed an inverse relation with the degree of heterozygosity.Several of the strains, and in particular those from Arpino, yielded asci that came from genetically different cells. These different cells could be interpreted to have arisen from a heterozygote that had sporulated and, because of the HO gene, yielded homozygous diploid spore clones. We propose that natural wine yeast strains can undergo such changes and thereby change a multiple heterozygote into completely homozygous diploids, some of which may replace the original heterozygous diploid. We call this process ‘genome renewal’.
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    The linkage of (1-3)-β-glucan to chitin during cell wall assembly in Saccharomyces cerevisiae (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 1591-1599 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chitin ; glucan ; cell wall synthesis ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Pulse-chase experiments with [14C]glucose demonstrated that in the cell wall of wild-type Saccharomyces cerevisiae alkali-soluble (1-3)-β-glucan serves as a precursor for alkali-insoluble (1-3)-β-glucan. The following observations support the notion that the insolubilization of the glucan is caused by linkage to chitin: (i) degradation of chitin by chitinase completely dissolved the glucan, and (ii) disruption of the gene for chitin synthase 3 prevented the formation of alkali-insoluble glucan. These cells, unable to form a glucan-chitin complex, were highly vulnerable to hypo-osmotic shock indicating that the linkage of the two polymers significantly contributes to the mechanical strength of the cell wall.Conversion of alkali-soluble glucan into alkali-insoluble glucan occurred both early and late during budding and also in the ts-mutant cdc24-1 in the absence of bud formation.
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    V. Yeast sequencing reports. UBP5 encodes a putative yeast ubiquitin-specific protease that is related to the human Tre-2 oncogene product (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 1497-1502 
    Details
    ISSN: 0749-503X
    Keywords: Ubiquitination ; protein turnover ; sequence homology ; oncogene ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A gene from chromosome V of the yeast Saccharomyces cerevisiae has been cloned and sequenced. The deduced amino acid sequence encoded by this gene is similar to several ubiquitin-specific proteases from yeast, especially at the highly conserved domain. It is thus named UBP5. UBP5 is also closely related to the human Tre-2 and the mouse Unp oncogene products. This study adds a new member to the ubiquitin protease family and suggests that alteration of ubiquitin protease activity may result in cancer in mammals. However, disruption of the UBP5 gene in a haploid strain did not result in a noticeable phenotypic alteration. The sequence has been deposited in the GenBank data library under Accession Number U10082.
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    IV. Yeast sequencing reports. Sequence of the PHO2-POL3 (CDC2) region of chromosome IV of Saccharomyces cerevisiae (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 1653-1656 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome IV ; POL3 (CDC2) ; KIN28 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The nucleotide sequence of a 5 kb EcoRI-NcoI fragment of chromosome IV, contiguous to gene POL3 (CDC2), has been determined. It contains three open reading frames: QRI1, QRI2 and QRI7. Two of them are essential genes. QRI7 is homologous to the Escherichia coli orfx gene. Accession number to EMBL/Genbank Data Library is X79380.
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    Selectable marker replacement in Saccharomyces cerevisiae (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 141-149 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; selectable marker ; transformation ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Selectable markers integrated by the ‘gamma’ deletion method (Sikorski and Hieter, 1989) can be efficiently replaced in vivo with other markers by transformation with homologous plasmids. Transformation frequencies in experiments designed to replace original selectable markers with an alternate marker were high and molecular analysis confirmed that all transformants that exhibited the expected phenotypes (loss of the original prototrophy and gain of the alternate prototrophy) resulted from homologous recombination between plasmid sequences at the target locus. This technique involves no plasmid construction and greatly facilitates the generation of yeast cells containing multiple gene disruptions.
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    Transport of hexoses in yeast. Re-examination of the sugar phosphorylation hypothesis with a new experimental approach (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 59-65 
    Details
    ISSN: 0749-503X
    Keywords: Hexose transport ; Saccharomyces cerevisiae ; glycolysis ; hexoses ; phosphorylation ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The constitutive transport of hexoses in yeast has been re-examined with a new radioactive experimental approach devised to distinguish between association or independence of the transport step with phosphorylation of the sugar substrate. The approach takes advantage of the fact that the label of [2-3H]mannose disappears once it has been phosphorylated by the yeast, due to its conversion to fructose-6-phosphate. Our results with wild-type yeast and this fermentable sugar support the view that the transport of hexoses in yeast does not involve phosphorylation of the substrate. Other features of the transport process have been examined using this experimental procedure and are also reported.
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    Purification of yeast histones competent for nucleosome assembly in vitro (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 319-331 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; histones ; nucleosome assembly ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have developed a procedure to purify nucleosomal assembly-competent histones as a mixture of H2A, H2B, H3 and H4 from isolated nuclei of the yeast Saccharomyces cerevisiae with a purity of 70-80%. The mixture contained each of the histone subunits approximately at the equi-molar ratio. Plasmid pBR322 DNA was assembled into nucleosomes with the purified yeast histones in the presence of nucleoplasmin from unfertilized eggs of the frog Xenopus laevis. The efficiency of assembly of yeast histones was comparable to that of core histones purified from HeLa cells. The length of DNA fragment wrapping around a core histone particle and the molar ratio of histone components in an assembled nucleosome particle were estimated to be 150 ± 10 bp long and H2A:H2B:H3:H4 = 1·0:0·9:0·9:1·0, respectively.
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    URL: http://dx.doi.org/10.1002/yea.320100305
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    Promoter analysis of the PDA1 gene encoding the E1α subunit of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 297-308 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; pyruvate dehydrogenase ; control of gene expression ; PDA1 ; GCN4 ; chromosome V ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The location and sequence of the PDA1 gene, encoding the E1α subunit of the pyruvate dehydrogenase (PDH) complex from Saccharomyces cerevisiae, were determined. The PDA1 gene was located on a 6·2 kb fragment of chromosome V, approximately 18 kb centromere distal to RAD3. Consistent with this, the PDA1 gene was genetically mapped at 4 cM from RAD3. A part of the 6·2 kb fragment of chromosome V was sequenced. The nucleotide sequence contained the PDA1 open reading frame and the entire putative promoter. Computer analysis revealed a putative GCN4 binding motif in the PDA1 promoter. The presence of transcriptional elements was experimentally determined by deletion analysis. To this end, ExoIII deletions were constructed in the 5′ to 3′ direction of the PDA1 promoter and effects on transcription were determined by Northern analysis. Transcription was unaffected upon deletion to position - 190 relative to the ATG start codon. Deletions from position - 148 and beyond, however, reduced promoter activity at least 40-fold. Apparently the 42 bp between nucleotides - 190 and - 148 contain an element essential for transcription. Inactivation of the PDA1 promoter could not be attributed to deletions of a recognizable TATA element or any known yeast regulatory motifs. The possible role of the CCCTT sequence present in the 42 bp region and also in the promoters of the other genes encoding subunits of the PDH complex is discussed.
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    A new family of yeast genes implicated in ergosterol synthesis is related to the human oxysterol binding protein (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 341-353 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; sterol biosynthesis ; oxysterol binding protein ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have identified three yeast genes, KES1, HES1 and OSH1, whose products show homology to the human oxysterol binding protein (OSBP). Mutations in these genes resulted in pleiotropic sterol-related phenotypes. These include tryptophan-transport defects and nystatin resistance, shown by double and triple mutants. In addition, mutant combinations showed small but apparently cumulative reductions in membrane ergosterol levels. The three yeast genes are also functionally related as overexpression of HES1 or KES1 alleviated the tryptophan-transport defect in kes1Δ or osh1Δ mutants, respectively. Our study implicates this new yeast gene family in ergosterol synthesis and provides comparative evidence of a role for human OSBP in cholesterol synthesis.
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    Positioning of cell growth and division after osmotic stress requires a map kinase pathway (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 425-439 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; morphogenesis ; MAP kinase ; osmotic stress ; cell division ; actin cytoskeleton ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The yeast Saccharomyces cerevisiae has a genetic program for selecting and assembling a bud site on the cell cortex. Yeast cells confine their growth to the emerging bud, a process directed by cortical patches of actin filaments within the bud. We have investigated how cells regulate budding in response to osmotic stress, focusing on the role of the high osmolarity glycerol response (HOG) pathway in mediating this regulation. An increase in external osmolarity induces a growth arrest in which actin filaments are lost from the bud. This is followed by a recovery phase in which actin filaments return to their original locations and growth of the original bud resumes. After recovery from osmotic stress, haploid cells retain an axial pattern of bud site selection while diploids change their bipolar budding pattern to an increased bias for forming a bud on the opposite side of the cell from the previous bud site. Mutants lacking the mitogen-activated protein (MAP) kinase encoded by HOG1 or the MAP kinase kinase encoded by PBS2 (previously HOG4) show a similar growth arrest after osmotic stress. However, in the recovery phase, the mutant cells (a) do not restart growth of the original bud but rather start a new bud, (b) fail to restore actin filaments to the original bud but move them to the new one, and (c) show a more random budding pattern. These defects are elicited by an increase in osmolarity and not by other environmental stresses (e.g., heat shock or change in carbon source) that also cause a temporary growth arrest and shift in actin distribution. Thus, the HOG pathway is required for repositioning of the actin cytoskeleton and the normal spatial patterns of cell growth after recovery from osmotic stress.
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    XIII. Yeast sequencing reports. Cloning and sequencing of the NES24 gene of Saccharomyces cerevisiae (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 371-376 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; NES24 ; chromosome XIII ; neomycin ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have cloned NES24 using a temperature-sensitive nes24-1 mutant as a host and sequenced a 3162 bp XhoI-EcoRI DNA fragment containing the NES24 gene. Computer analysis revealed that this segment contains a 1806 bp open reading frame which is needed for complementation of the nes24-1 mutation. We found SUP8 in the region upstream of the NES24 gene, placing the NES24 gene on chromosome XIII. A protein homology search indicated that NES24 encodes a new protein. The disruption of the NES24 gene resulted in temperature-sensitive growth. The sequence has been deposited in DDBJ/EmBL/GenBank data bases under Accession Number D15052.
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    V. Yeast sequencing reports. Identification of a gene encoding a new Ypt/Rab-like monomeric G-protein in Saccharomyces cerevisiae (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 399-402 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; Chromosome V ; Monomeric G-protein ; Rab protein ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A Saccharomyces cerevisiae sequence cloned by serendipity was found to encode a protein that is a new member of the Ypt/Rab monomeric G-protein family. This sequence shows high homology to the yeast genes SEC4 and YPT1 and, like SEC4 and YPT1, is essential for viability. The sequence was localized to chromosome V based upon hybridization to pulse-field gel-separated yeast chromosomes. The sequence has been deposited in the GenBank data library under Accession Number L17070.
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    II. Yeast sequencing reports. The two genes encoding yeast ribosomal protein S8 reside on different chromosomes, and are closely linked to the hsp70 stress protein genes SSA3 and SSA4 (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 1093-1100 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome II ; sequencing ; ribosomal protein ; intron ; hsp 70 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A 7·4 kb segment of chromosome II was sequenced and analysed. This segment is part of the 25 kb insert of cosmid clone α1004.10 which is located on the left arm of chromosome II. Sequence analysis revealed four open reading frames (ORFs), of which two had been characterized previously (SSA3, AAR2) and one was not identified. The other ORF was precisely 600 bp long and the deduced protein sequence predicted a very basic protein (pI=11·1; molecular weight=22·5 kDa). Evidence was found that the ORF is the S40 ribosomal protein gene (RPG) S8. Consensus splice signals were found in the 5′ leader sequence and also potential RPG-specific sequences. Chromoblot analysis revealed a second copy of the S8 RPG on chromosome IV or VIII. This copy is also closely linked to an hsp70 protein gene, SSA4. The sequence has been deposited in the EMBL data library under accession number Z26879.
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    Formation of poliomyelitis subviral particles in the yeast Saccharomyces cerevisiae (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 907-922 
    Details
    ISSN: 0749-503X
    Keywords: Poliovirus ; subviral particles ; posttranslational cleavage ; heterologous gene expression ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The sequence of the poliovirus genome encoding 3CD (a protease) was transferred to the yeast Saccharomyces cerevisiae on expression vectors with either a constitutive or an inducible promoter. Transformants could only be obtained with vectors carrying the inducible transcription unit. Extracts of induced cells were able to cleave cell-free synthesized P1, the precursor of the poliovirus capsid proteins, into VP0, VP3 and VP1.In yeast cells constitutively expressing P1, induction of 3CD expression resulted in only trace amounts of processed products. Processing could be improved considerably by simultaneous induction of both P1 and 3CD expression. Analysis of extracts of such induced cells revealed the presence of particles that resembled authentic subviral particles.
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    X. Yeast sequencing reports. Sequence and function analysis of a 9·46 kb fragment of Saccharomyces cerevisiae chromosome X (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 965-973 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome X ; BCK1 ; SLK1 ; RADH ; transposon-facilitated DNA sequencing ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In the framework of the European yeast genome sequencing project, we have determined the nucleotide sequence of the cosmid clone 233 provided by F. Galibert (Rennes Cedex, France). We present here 9464 base pairs of this cosmid located on the left arm of Saccharomyces cerevisiae chromosome X. This sequence contains two new open reading frames and includes the published sequences of the RADH gene (also identified as SRS2/HPR5) and the 3′-end of the gene BCK1/SLK1/SSP31. Deletion mutants of the two unknown genes J0909 and J0911 are viable. The sequence has been deposited in the EMBL data library under accession number X77087.
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    XIV. Yeast sequencing reports. Sequence of MKT1, needed for propagation of M2 satellite dsRNA of the L-A virus of Saccharomyces cerevisiae (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 1477-1479 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; MKT1 ; killer maintenance ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: MKT1 is required for maintenance of K2 above 30°C in strains with the L-A-HN variant of the L-A double-stranded RNA virus of Saccharomyces cerevisiae. We report that MKT1 encodes a 92 979 Da protein with serine-rich regions and the retroviral protease signature, DTG, but with no substantial homology to proteins presently in the databases. This sequence is available from GenBank under Accession Number U09129.
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    Effect of site-directed mutagenesis of conserved lysine residues upon Pas1 protein function in peroxisome biogenesis (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 1613-1620 
    Details
    ISSN: 0749-503X
    Keywords: Peroxisome ; yeast ; Saccharomyces cerevisiae ; site-directed mutagenesis ; AAA-family ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The Pas1 protein (Pas1p) is required for peroxisome biogenesis in Saccharomyces cerevisiae and contains two putative ATP-binding sites, each within a domain which is conserved among members of the recently characterized AAA-family. To elucidate whether both putative ATP-binding sites are essential for Pas1p function, lysine467 of the first and lysine744 of the second putative ATP-binding site were each changed to glutamate by site-directed mutagenesis. While replacement of lysine744 abolished the function of the Pas1 protein in peroxisome biogenesis, replacement of lysine467 had no obvious effect.
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    II. Yeast sequencing reports. Analysis of a 17·4 kb DNA segment of yeast chromosome II encompassing the ribosomal protein L19 as well as proteins with homologies to components of the hnRNP and snRNP complexes and to the human proliferation-associated p120 antigen (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 1663-1673 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; chromosome II ; MCM2 ; AAC2 ; KH motif ; hnRNP ; snRNP ; SMD1 ; ribosomal protein ; RL19 ; intron ; leucine zipper ; proliferation-associated antigen ; ARS ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We report the nucleotide sequence of a 17·4 kb DNA segment from the left arm of Saccharomyces cerevisiae chromosome II. This sequence contains 12 open reading frames (ORFs) longer than 300 bp and a putative autonomously replicating sequence (ARS). The ORF YBL0418 contains the KH motif present in several nucleic acid-binding proteins and shares homologies with the mouse X protein of the heterogeneous nuclear ribonucleo-protein (hnRNP) complexes involved in pre-mRNA processing. YBL0424 is the yeast member of the ribosomal protein L19 (YL14) family. YBL0425 is related to the D1 core polypeptide of the small nuclear ribonucleoprotein (snRNP) particles involved in the splicing of introns. YBL0437 is a putative homologue of the human protein p120, one of the major antigens associated with malignant tumours. Mcm2, a protein important for ARS activity, as well as Aac2, one of the three isoforms of the mitochondrial ATP/ADP carrier, were previously described (Yan et al., 1991; Lawson and Douglas, 1988). Four ORFs show no homology or particular features that could help to assess their functions. The last ORFs are not likely to be expressed for they are localized on the complementary strand of longer ORFs. The sequence has been submitted to the EMBL data library under Accession Number X77291.
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    XI. Yeast sequencing reports. The complete sequence of an 18,002 bp segment of Saccharomyces cerevisiae chromosome XI contains the HBS1, MRP-L20 and PRP16 genes, and six new open reading frames (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 231-245 
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    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; genome sequencing ; chromosome XI ; HBS1 ; MRP-L20 ; PRP16 ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We report the sequence of an 18,002 bp DNA fragment from the right arm of Saccharomyces cerevisiae chromosome XI. This segment contains nine complete open reading frames (ORFs), YKR401 to YKR409, and part of another ORF, YKR400, covering altogether 87·2% of the entire sequence. One of them, YKR400, encodes an NAD-dependent 5,10-methylene-tetrahydrofolate dehydrogenase. YKR404, YKR405 and YKR406 correspond to the previously characterized HBS1, MRP-L20 and PRP16 genes, coding for a translation elongation factor, a mitochondrial ribosomal protein and an ATP-binding protein, respectively. The putative product of YKR407 contains the zinc-binding region signature of neutral zinc metallopeptidases. The five other ORFs do not show significant homology to any known protein. The sequence data reported here have been assigned EMBL accession number Z27116.
    Additional Material: 8 Ill.
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    URL: http://dx.doi.org/10.1002/yea.320100210
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    Purification of properties of Saccharomyces cerevisiae cystathionine β-synthase (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 333-339 
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    ISSN: 0749-503X
    Keywords: Cystathionine ; β-synthase ; enzyme purification ; amino acid sequence analysis ; catalytic properties ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Cystathionine β-synthase (β-CTSase), which catalyses cystathionine synthesis from serine and homocysteine, was purified to homogeneity from Saccharomyces cerevisiae. The molecular mass of the enzyme was estimated to be 235 kDa by gel filtration and 55 kDa by sodium dodecyl sulphate-polyacrylamide gel electrophoresis, indicating that it is a homotetramer. The N-terminal amino acid sequence of the enzyme perfectly coincided with that deduced from the nucleotide sequence of CYS4, except for the absence of initiation methionine. The purified β-CTSase catalysed cysteine synthesis from serine (or O-acetylserine) and H2S. From this finding, we discuss the multifunctional nature and evolutionary divergence of S-metabolizing enzymes.
    Additional Material: 3 Ill.
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    URL: http://dx.doi.org/10.1002/yea.320100306
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    XV. Yeast sequencing reports. A gene from Saccharomyces cerevisiae which codes for a protein with significant homology to the bacterial 3-phosphoserine aminotransferase (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 385-389 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; serine biosynthesis ; ser1 ; chromosome XV ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: During the sequencing of the gene GSP2 from Saccharomyces cerevisiae, we have encountered an adjacent open reading frame having strong homology to the 3-phosphoserine aminotransferase (E.C.2.6.1.52) from other organisms. In this report, we present the sequence for this yeast SERC, and evidence that its deletion from the yeast genome leads to serine dependency. The sequence has been deposited in the GenBank data library under Accession Number L20917.
    Additional Material: 3 Ill.
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    URL: http://dx.doi.org/10.1002/yea.320100311
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    Yeast sequencing reports. APL1, a yeast gene encoding a putative permease for basic amino acids (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 653-657 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; basic-amino-acid permease ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A Saccharomyces cerevisiae gene (1722 bp), encoding a protein (574 aa) highly homologous to the basic-amino-acid permeases LYP1 and CAN1, was sequenced. The gene, which was named APL1 (Amino-acid Permase Like), is located 881 bp upstream from LYP1 (lysine-specific permease), and in head-to-head orientation to it. These sequence data have been deposited in the EMBL/GenBank/DDBJ nucleotide sequence data libraries under Accession Number X74069.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/yea.320100509
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    XI. Yeast sequencing reports. The complete sequencing of a 24·6 kb segment of yeast chromosome XI identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open reading frames including homologues to the threonine dehydratases, membrane transporters, hydantoinases and the phospholipase A2-activating protein (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 663-679 
    Details
    ISSN: 0749-503X
    Keywords: Genome sequencing ; Saccharomyces cerevisiae ; chromosome XI ; catabolic threonine dehydratase ; membrane transporter ; hydantoinase ; phospholipase A2-activating protein ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We report the entire sequence of a 26·4 kb segment of chromosome XI of Saccharomyces cerevisiae. Identification of the known loci URA1, TRP3 and SAC1 revealed a translocation compared to the genetic map. Additionally, six unknown open reading frames have been identified. One of them is similar to catabolic threonine dehydratases. Another one contains characteristic features of membrane transporters. A third one is homologous in half of its length to the prokaryotic hydantoinase HyuA and in the other half to hydatoinase HyuB. A fourth one is homologous to the mammalian phospholipase A2-activating protein. A fifth one, finally, is homologous to the hypothetical open reading frame YCR007C of chromosome III. The sequence has been deposited in the EMBL data library under Accession Number X75951.
    Additional Material: 7 Ill.
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    URL: http://dx.doi.org/10.1002/yea.320100511
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    Genetic evidence for a functional interaction between Saccharomyces cerevisiae CDC24 and CDC42 (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 10 (1994), S. 463-474 
    Details
    ISSN: 0749-503X
    Keywords: Saccharomyces cerevisiae ; cell polarity ; cellular morphogenesis ; GTPases ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Cdc24p and Cdc42p are involved in the control of cell polarity during the Saccharomyces cerevisiae cell cycle. Cdc42p is a member of the Ras superfamily of GTPases and Cdc24p displays limited amino-acid sequence similarity with the Dbl proto-oncoprotein, which acts to stimulate guanine-nucleotide exchange on human Cdc42p. We have performed several genetic experiments to test whether Cdc24p and Cdc42p interact within the cell. First, overexpression of Cdc24p suppressed the dominant-negative cdc42D118A allele. Second, overexpression of wild-type CDC24 and CDC42 genes together was a lethal event resulting in a morphological phenotype of large, round, unbudded cells, indicating a loss of cell polarity. Third, a cdc24ts cdc42ts double mutant exhibited a synthetic-lethal phenotype at the semi-permissive temperature of 30°C. These data suggest that Cdc24p and Cdc42p interact within the cell and that Cdc24p may be involved in the regulation of Cdc42p activity.
    Additional Material: 4 Ill.
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    URL: http://dx.doi.org/10.1002/yea.320100405
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