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  • Saccharomyces cerevisiae  (243)
  • Springer  (243)
  • 2020-2024
  • 1990-1994  (243)
  • 101
    Electronic Resource
    Electronic Resource
    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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  • 102
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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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  • 103
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    Intracellular pH inSchizosaccharomyces pombe — Comparison withSaccharomyces cerevisiae (1993)
    Springer
    Molecular and cellular biochemistry 124 (1993), S. 131-140 
    Details
    ISSN: 1573-4919
    Keywords: Schizosaccharomyces pombe ; Saccharomyces cerevisiae ; H+-ATPase ; intracellular pH ; carboxy-seminaphthorhodafluor-1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract We examined cytoplasmic pH regulation inSchizosaccharomyces pombe andSaccharomyces cerevisiae using pH-sensitive fluorescent dyes. Of several different fluorescent compounds tested, carboxy-seminaphthorhodafluor-1 (C.SNARF-1) was the most effective. Leakage of C.SNARF-1 fromS. pombe was much slower than leakage fromC. cerevisiae. Using the pH-dependent fluorescence of C.SNARF-1 we showed that at an external pH of 7, mean resting internal pH was 7.0 forS. pombe and 6.6 forS. cerevisiae. We found that internal pH inS. pombe was maintained over a much narrower range in response to changes in external pH, especially at acidic pH. The addition of external glucose caused an intracellular alkalinization in both species, although the effect was much greater inS. cerevisiae than inS. pombe. The plasma membrane H+-ATPase inhibitor diethylstilbestrol reduced both the rate and extent of alkalinisation, with an IC50 of approximately 35 μM in both species. Amiloride also inhibited internal alkalinisation with IC50's of 745 μM forS. cerevisiae and 490 μM forS. pombe.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00929205
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  • 104
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    Expression of a functionally active cardiac fatty acid-binding protein in the yeast, Saccharomyces cerevisiae (1990)
    Springer
    Molecular and cellular biochemistry 98 (1990), S. 69-74 
    Details
    ISSN: 1573-4919
    Keywords: bovine heart fatty acid-binding protein ; H-FABPc ; heterologous gene expression ; Saccharomyces cerevisiae ; GALIO promoter
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary The unicellular eukaryotic microorganism, Saccharomyces cerevisiae, transformed with a plasmid containing a cDNA fragment encoding bovine heart fatty acid-binding protein (H-FABP) under the control of the inducible yeast GAL10 promoter, expressed FABP during growth on galactose. The maximum level of immunoreactive FABP, identical in size to native protein as judged from SDS-polyacrylamide gel electrophoresis, was reached after approximately 16 hours of induction. Analysis of particulate and soluble subcellular fractions showed that FABP was exclusively associated with the cytosol. FABP expressed in yeast cells was functional as was demonstrated by its capacity to bind 14C-oleic acid in an in vitro assay. Growth of the transformants on galactose as the carbon source was significantly retarded at 37°C. Whereas the fatty acid pattern of total lipids was not altered in transformed cells, desaturation of exogenously added 14C-palmitic acid was significantly reduced both at 30 and 37°C. The lowest percentage of radioactively labeled unsaturated fatty acids was found in the phospholipid fraction.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00231369
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  • 105
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    Metals are directly involved in the redox interconversion of Saccharomyces cerevisiae glutathione reductase (1991)
    Springer
    Molecular and cellular biochemistry 101 (1991), S. 175-187 
    Details
    ISSN: 1573-4919
    Keywords: glutathione reductase ; Saccharomyces cerevisiae ; redox interconversion ; metals ; cell-free extracts
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Redox inactivation of glutathione reductase involves metal cations, since chelators protected against NADPH-inactivation, 3 µM EDTA or 10 µM DETAPAC yielding full protection. Ag+, Zn2+ and Cd2+ potentiated the redox inactivation promoted by NADPH alone, while Cr3+, Fe2+, Fe3+, Cu+, and Cu2+ protected the enzyme. The Zn2+ and Cd2+ effect was time-dependent, unlike conventional inhibition. Glutathione reductase interconversion did not require dioxygen, excluding participation of active oxygen species produced by NADPH and metal cations. One Zn2+ ion was required per enzyme subunit to yield full NADPH-inactivation, the enzyme being reactivated by EDTA. Redox inactivation of glutathione reductase could arise from the blocking of the dithiol formed at the active site of the reduced enzyme by metal cations, like Zn2+ or Cd2+. The glutathione reductase activity of yeast cell-free extracts was rapidly inactivated by low NADPH or moderate NADH concentrations; NADP+ also promoted rapid inactivation in fresh extracts, probably after reduction to NADPH. Full inactivation was obtained in cell-free extracts incubated with glucose-6-phosphate or 6-phosphogluconate; the inactivating efficiency of several oxidizable substrates was directly proportional to the specific activities of the corresponding dehydrogenases, confirming that redox inactivation derives from NADPH formed in vitro.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00229534
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  • 106
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    Antibodies raised against yeast HSP 104 cross-react with a heat-and abscisic acid-regulated polypeptide in rice (1993)
    Springer
    Plant molecular biology 22 (1993), S. 1177-1180 
    Details
    ISSN: 1573-5028
    Keywords: abscisic acid ; developmental regulation ; heat shock proteins ; Oryza sativa ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Antibodies raised against yeast heat shock protein (HSP) 104 recognized a heat-inducible polypeptide with a molecular mass of 110 kDa in shoot tissue of young rice seedlings. Root tissue of the same age showed no immuno-reaction with yeast HSP 104 antibodies. The 110 kDa polypeptide of rice was also shown to be abscisic acid-inducible in young seedlings. Though this polypeptide was seen to be constitutively present in the flag leaf of 90-day-old field-grown plant, it was not much affected by either heat shock or abscisic acid in this case.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00028989
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  • 107
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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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00990545
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  • 108
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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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00019499
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  • 109
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    Fluorescence staining of yeast cells permeabilized by killer toxin K1: Determination of optimum conditions (1993)
    Springer
    Journal of fluorescence 3 (1993), S. 241-244 
    Details
    ISSN: 1573-4994
    Keywords: Killer toxin K1 ; bromocresol purple staining ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract Optimal assay conditions were established for the previously described method used to determine the activity ofSaccharomyces cerevisiae pore-forming killer toxin K1. The method is based on cell staining with bromocresol purple. Sensitive cells ofS. cerevisiae from the early exponential phase under nongrowth conditions and in the presence of glucose were the most convenient for determining the killer toxin activity. Maximum killing war reached when the suspension was buffered with 10 mM citrate-phosphate at pH 4.6.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00865270
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  • 110
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    Cloning of a cDNA for rape chloroplast 3-isopropylmalate dehydrogenase by genetic complementation in yeast (1992)
    Springer
    Plant molecular biology 18 (1992), S. 557-566 
    Details
    ISSN: 1573-5028
    Keywords: Brassica napus ; chloroplast ; 3-isopropylmalate dehydrogenase ; molecular evolution ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Both insect and mammalian genes have previously been cloned by genetic complementation in yeast. In the present report, we show that the method can be applied also to plants. Thus, we have cloned a rape cDNA for 3-isopropylmalate dehydrogenase (IMDH) by complementation of a yeast leu2 mutation. The cDNA encodes a 52 kDA protein which has a putative chloroplast transit peptide. The in vitro made protein is imported into chloroplasts, concomitantly with a proteolytic cleavage. We conclude that the rape cDNA encodes a chloroplast IMDH. However, Southern analysis revealed that the corresponding gene is nuclear. In a comparison of IMDH sequences from various species, we found that the rape IMDH is more similar to bacterial than to eukaryotic proteins. This suggests that the rape gene could be of chloroplast origin, but has moved to the nucleus during evolution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00040671
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  • 111
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    Genetic analysis of clathrin function in yeast (1990)
    Springer
    The journal of membrane biology 116 (1990), S. 93-105 
    Details
    ISSN: 1432-1424
    Keywords: clathrin ; genetics ; Saccharomyces cerevisiae ; exocytosis ; endocytosis ; prohormone maturation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01868668
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  • 112
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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 
    Details
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00280191
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  • 113
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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 
    Details
    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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00290110
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  • 114
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    Growth-related expression of ribosomal protein genes in Saccharomyces cerevisiae (1993)
    Springer
    Molecular genetics and genomics 239 (1993), S. 196-204 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Ribosomal protein genes ; Transcription activation ; cAMP ; Growth control
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The rate of ribosomal protein gene (rp-gene) transcription in yeast is accurately adjusted to the cellular requirement for ribosomes under various growth conditions. However, the molecular mechanisms underlying this co-ordinated transcriptional control have not yet been elucidated. Transcriptional activation of rp-genes is mediated through two different multifunctional trans-acting factors, ABF1 and RAP1. In this report, we demonstrate that changes in cellular rp-mRNA levels during varying growth conditions are not parallelled by changes in the in vitro binding capacity of ABF1 or RAP1 for their cognate sequences. In addition, the nutritional upshift response of rp-genes observed after addition of glucose to a culture growing on a non-fermentative carbon source turns out not to be the result of increased expression of the ABF1 and RAP1 genes or of elevated DNA-binding activity of these factors. Therefore, growth rate-dependent transcription regulation of rp-genes is most probably not mediated by changes in the efficiency of binding of ABF1 and RAP1 to the upstream activation sites of these genes, but rather through other alterations in the efficiency of transcription activation. Furthermore, we tested the possibility that cAMP may play a role in elevating rp-gene expression during a nutritional shift-up. We found that the nutritional upshift response occurs normally in several mutants defective in cAMP metabolism.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00281618
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  • 115
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    Inducible removal of UV-induced pyrimidine dimers from transcriptionally active and inactive genes of Saccharomyces cerevisiae (1993)
    Springer
    Molecular genetics and genomics 239 (1993), S. 28-32 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; UV damage ; Mating type ; Inducible repair
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The prior UV irradiation of α haploid Saccharomyces cerevisiae with a UV dose of 25 J/m2 substantially increases the repairability of damage subsequently induced by a UV dose of 70 J/m2 given 1 h after the first irradiation. This enhancement of repair is seen at both the MATa and HMLα loci, which are, respectively, transcriptionally active and inactive in α haploid cells. The presence in the medium of the protein synthesis inhibitor, cycloheximide in the period between the two irradiations eliminated this effect. Enhanced repair still occurred if cycloheximide was present only after the final UV irradiation. This indicated that the first result is not due to cycloheximide merely blocking the synthesis of repair enzymes associated with a hypothetical rapid turnover of such molecules. The enhanced repairability is not the result of changes in chromatin accessibility without protein synthesis, merely caused by the repair of the damage induced by the prior irradiation. The data clearly show that a UV-inducible removal of pyrimidine dimers has occurred which involves the synthesis of new proteins. The genes known to possess inducible promoters, and which are involved in excision are RAD2, RAD7, RAD16 and RAD23. Studies with the rad7 and rad16 mutants which are defective in the ability to repair HMLα and proficient in the repair' of MATα showed that in rad7, preirradiation enhanced the repair at MATα, whereas in rad16 this increased repair of MATα was absent. The preirradiation did not modify the inability to repair HMLα in either strain. Thus RAD16 has a role in this inducible repair. Inducible repair is also absent in a rad2 strain which cannot repair MATα or HMLα after a single UV dose.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00281597
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  • 116
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    Yeast calmodulin localizes to sites of cell growth (1992)
    Springer
    Protoplasma 166 (1992), S. 110-113 
    Details
    ISSN: 1615-6102
    Keywords: Calmodulin ; Ca2+ ; Cell polarity ; Budding yeast ; Saccharomyces cerevisiae ; Microfilament
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Intracellular localization of calmodulin was examined in the budding yeast,Saccharomyces cerevisiae. Distribution of calmodulin changes in a characteristic way during the cell cycle. Calmodulin localizes to a patch at the presumptive bud site of unbudded cells. It concentrates at the bud tip in small-budded cells, and later it diffuses throughout the entire bud. At cytokinesis, calmodulin is largely at the neck between the mother and daughter cells. Double staining experiments have shown that the location of some polarized actin dots is coincident with that of calmodulin dots. Polarized localization of actin dots is observed in cells depleted of calmodulin, suggesting that calmodulin is not required for localization of the actin dots. Thecdc24 mutant that has a defect in bud assembly at the restrictive temperature fails to exhibit polarized localization of calmodulin, indicating that theCDC24 gene product is responsible for controlling the polarity of calmodulin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01320150
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  • 117
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    Eukaryotic glucose-6-phosphate dehydrogenases: Structural screening of related proteins (1991)
    Springer
    The protein journal 10 (1991), S. 25-29 
    Details
    ISSN: 1573-4943
    Keywords: Screening protein structures ; electroblotting ; glucose-6-phosphate dehydrogenase ; Saccharomyces cerevisiae ; Pichia jadinii
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Rapid assessment of structural relationships between yeast glucose-6-phosphate dehydrogenases and other eukaryotic types of this enzyme is described. Separation and size estimation of large fragments by sodium dodecylsulfate/polyacrylamide gel electrophoresis, electroblotting onto disks, and sequencer analysis provide data that permit alignment of the segments thus characterized with the related proteins, and utilize existing structural knowledge to assess new enzyme structures. Affinity labeling allows further correlations. The results establish the overall structural arrangements of the new proteins, including the location of the active-site lysine residue, even though the yeast enzyme structures are found to differ markedly from the few previously characterized glucose-6-phosphate dehydrogenases.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024652
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  • 118
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    Identification of a site required for DNA replication fork blocking activity in the rRNA gene cluster in Saccharomyces cerevisiae (1992)
    Springer
    Molecular genetics and genomics 233 (1992), S. 355-362 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Replication fork block ; rRNA gene ; 2 gm Plasmid ; 2D agarose gel electrophoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The yeast genome has DNA replication fork blocking sites, that we have named sog sites, in the ribosomal RNA gene (rDNA) cluster. These are located at the 3′ end of the 35S rRNA transcription unit and they block replication fork movement in a direction opposite to that of RNA polymerase I. We cloned this replication blocking site into a YEp-type plasmid and analyzed DNA replication intermediates, using two-dimensional (2D) agarose gel electrophoresis. The blocking activity remained even on a plasmid not involved in 35S rRNA transcription and inhibited fork movement in the same polar fashion as on the yeast chromosome. To define the site further, smaller fragments were subcloned into the YEp-type plasmid. A small 109 by region exhibited sog activity and was located near the enhancer region for 35S rRNA transcription. It overlaps an essential element of the recombinational hot spot HOT1.
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    URL: http://dx.doi.org/10.1007/BF00265431
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  • 119
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    TFS1: A suppressor of cdc25 mutations in Saccharomyces cerevisiae (1991)
    Springer
    Molecular genetics and genomics 230 (1991), S. 241-250 
    Details
    ISSN: 1617-4623
    Keywords: Yeast ; Saccharomyces cerevisiae ; Adenylyl cyclase ; CDC25 ; RAS
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The TFS1 gene of Saccharomyces cerevisiae is a dosage-dependent suppressor of cdc25 mutations. Overexpression of TFS1 does not alleviate defects of temperature-sensitive adenylyl cyclase (cdc35) or ras2 disruption mutations. The ability of TFS1 to suppress cdc25 is allele specific: the temperature-sensitive cdc25-1 mutation is suppressed efficiently but the cdc25-5 mutation and two disruption mutations are only partially suppressed. TFS1 maps to a previously undefined locus on chromosome XII between RDN1 and CDC42. The DNA sequence of TFS1 contains a single long open reading frame encoding a 219 amino acid polypeptide that is similar in sequence to two mammalian brain proteins. Insertion and deletion mutations in TFS1 are haploviable, indicating that TFS1 is not essential for growth.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00290674
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  • 120
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    Ty RNA levels determine the spectrum of retrotransposition events that activate gene expression in Saccharomyces cerevisiae (1990)
    Springer
    Molecular genetics and genomics 220 (1990), S. 213-221 
    Details
    ISSN: 1617-4623
    Keywords: Ty elements ; Saccharomyces cerevisiae ; Retrotransposon
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary To learn more about the variety of Ty elements capable of activating gene expression, we characterized 206 spontaneous Ty transpositions that activate the promoterless gene his3Δ4. Most of the Ty elements appear to be full-length, although a few deleted elements were recovered. Over 95% of the insertions belong to the Ty1 family, and the rest are Ty2 elements. The excessive number of Ty1 transpositions was unexpected because there are only 2-fold more Ty1 than Ty2 elements in the yeast strains used in the selection. However, there is 20-fold more Ty1 than Ty2 RNA present in these yeast strains. This difference in RNA level explains the greater number of Ty1 verses Ty2 transpositions at his3Δ4, because Ty elements transpose through an RNA intermediate. A similar association between the Ty transcript level and transpositional activation of his3Δ4 is obtained in cells expressing GAL1-promoted Ty2-H556 or Ty2-917 elements, but only if the element does not contain a marker. Genetically marked Ty2-H556NEO and-917NEO elements transpose into and activate his3Δ4 with the same efficiency as the previously characterized Ty1H3NEO element, but are underrepresented relative to the levels of TyNEO transcript. We also found that chromosomal Ty transcripts are even more abundant than previously estimated and comprise about 1% of total cellular RNA.
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    URL: http://dx.doi.org/10.1007/BF00260484
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    Molecular structure of the DNA cross-link repair gene SNM1(PSO2) of the yeast Saccharomyces cerevisiae (1992)
    Springer
    Molecular genetics and genomics 231 (1992), S. 194-200 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; DNA repair ; Nitrogen mustard ; Interstrand cross-links ; Nucleotide sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A 3.2 kb yeast DNA fragment containing the DNA interstrand cross-link-specific repair gene SNM1 has been sequenced. Two genes were identified. SNM1 has an open reading frame of 1983 by and codes for a 661 amino acid protein. Hydrophobic analysis shows that the protein is most probably not directly membrane bound. The second gene, UGX1, has an open reading frame of 573 by coding for a polypeptide of 191 amino acid residues. The two genes are arranged head to head and share a 192 by divergent promoter region that contains three TATAAA motives, two for the SNM1 and one for the UGX1 locus. Gene UGX1 has no apparent influence on the sensitivity of the cell to cross-linking nitrogen mustard, as its disruption in wild type does not increase sensitivity to nitrogen mustard and the presence of multiple copies of the gene fails to complement the nitrogen mustard sensitivity phenotype of snm1 disruption mutants. Northern analysis revealed that the expression of SNM1 yields an average of 0.3 copies/cell of a 2.4 kb transcript, while expression of UGX1 yields higher levels of a 0.8 kb poly(A)+ RNA.
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    URL: http://dx.doi.org/10.1007/BF00279791
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    Chromatin structure of the yeast SUC2 promoter in regulatory mutants (1992)
    Springer
    Molecular genetics and genomics 231 (1992), S. 395-400 
    Details
    ISSN: 1617-4623
    Keywords: SUC2 ; Saccharomyces cerevisiae ; Chromatin ; Micrococcal nuclease ; Promoter
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have previously suggested that two positioned nucleosomes are removed from the promoter of the Saccharomyces cerevisiae SUC2 gene upon derepression by glucose starvation. To gain further insight into the changes accompanying derepression at the chromatin level we have studied the chromatin structure of the SUC2 promoter in several mutants affecting SUC2 expression. The non-derepressible mutants snf1, snf2 and snf5 present a chromatin structure characteristic of the repressed state, irrespective of the presence or absence of glucose. The non-repressible mutants, mig1 and ssn6, as well as the double mutant snfs sn6 exhibit an opened chromatin structure even in the presence of glucose. These results suggest that the DNA-binding protein encoded by MIG1 is necessary to produce the characteristic pattern of repressed chromatin and that the SNF1 protein kinase is sufficient to produce the derepressed chromatin pattern. A model is presented for the transitions that result in opening up of the chromatin structure.
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    URL: http://dx.doi.org/10.1007/BF00292708
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    Conjugative transfer and autonomous replication of a promiscuous IncQ plasmid in the cyanobacterium Synechocystis PCC 6803 (1990)
    Springer
    Molecular genetics and genomics 221 (1990), S. 129-133 
    Details
    ISSN: 1617-4623
    Keywords: Bacterial conjugation ; Cyanobacteria ; IncQ plasmids ; Saccharomyces cerevisiae ; DNA methylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The promiscuous IncQ plasmid pKT210 (Cmr, Smr) is efficiently transferred by transpecific conjugation from Escherichia coli to the facultatively heterotrophic cyanobacterium Synechocystis PCC6803 when mobilized by a helper plasmid coding for IncP transfer functions. The IncQ plasmid is stably maintained in the cyanobacterium as an autonomously replicating multicopy plasmid with no detectable structural alterations and can be recovered by transformation back to E. coli when using a mcrA mcrB host. Thus, the replicative host-range of IncQ plasmids extends beyond purple bacteria to the distinct procaryotic taxon of cyanobacteria, allowing the use of these small plasmids as convenient cloning vectors in Synechocystis PCC6803 and presumably also in cyanobacteria that are not amenable to genetic transformation. In contrast, an IncQ plasmid bearing the TRP1 gene of Saccharomyces cerevisiae failed to replicate when transferred to that yeast by transformation.
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    URL: http://dx.doi.org/10.1007/BF00280378
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    Differential expression of two genes encoding isoforms of the ATPase involved in sodium efflux in Saccharomyces cerevisiae (1993)
    Springer
    Molecular genetics and genomics 236 (1993), S. 363-368 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Sodium efflux ; Lithium efflux ; ATPase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The ENA2 gene encoding a P-type ATPase involved in Na+ and Li+ effluxes in Saccharomyces cerevisiae has been isolated. The putative protein encoded by ENA2 differs only in thirteen amino acids from the protein encoded by ENA1/PMR2. However, ENA2 has a very low level of expression and for this reason did not confer significant Li+ tolerance on a Li+ sensitive strain. ENA1 and ENA2 are the first two units of a tandem array of four highly homologous genes with probably homologous functions.
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    URL: http://dx.doi.org/10.1007/BF00277134
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    Post-transcriptional regulation of IME1 determines initiation of meiosis in Saccharomyces cerevislae (1993)
    Springer
    Molecular genetics and genomics 237 (1993), S. 375-384 
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    ISSN: 1617-4623
    Keywords: Regulation of meiosis ; Saccharomyces cerevisiae ; IME1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The IME1 gene of Saccharomyces cerevisiae is required for initiation of meiosis. Transcription of IME1 is detected under conditions which are known to induce initiation of meiosis, namely starvation for nitrogen and glucose, and the presence of MATa1 and MATα2 gene products. In this paper we show that IME1 is also subject to translational regulation. Translation of IME1 mRNA is achieved either upon nitrogen starvation, or upon G1 arrest. In the presence of nutrients, constitutively elevated transcription of IME1 is also sufficient for the translation of IME1 RNA. Four different conditions were found to cause expression of Imel protein in vegetative cultures: elevated transcription levels due to the presence of IME1 on a multicopy plasmid; elevated transcription provided by a Gal-IME1 construct; G1 arrest due to α-factor treatment; G1 arrest following mild heat-shock treatment of cdc28 diploids. Using these conditions, we obtained evidence that starvation is required not only for transcription and efficient translation of IME1, but also for either the activation of Ime1 protein or for the induction/activation of another factor that, either alone or in combination with Ime1, induces meiosis.
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    URL: http://dx.doi.org/10.1007/BF00279441
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    Molecular and genetic characterization of SPT4, a gene important for transcription initiation in Saccharomyces cerevisiae (1993)
    Springer
    Molecular genetics and genomics 237 (1993), S. 449-459 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Transcription ; spt mutants
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutations in the SPT4 gene of Saccharomyces cerevisiae were isolated as suppressors of δ insertion mutations that interfere with adjacent gene transcription. Recent genetic evidence indicates that the SPT4 protein functions with two other proteins, SPT5 and SPT6, in some aspect of transcription initiation. In this work we have characterized the SPT4 gene and we demonstrate that spt4 mutations, like spt5 and spt6 mutations, cause changes in transcription. Using the cloned SPT4 gene, spt4 null mutations were constructed; in contrast to spt5 and spt6 null mutants, which are inviable, spt4 null mutants are viable and have an Spt− phenotype. The DNA sequence of the SPT4 gene predicts a protein product of 102 amino acids that contains four cysteine residues positioned similarly to those of zinc binding proteins. Mutational analysis suggests that at least some of these cysteines are essential for SPT4 function. Genetic mapping showed that SPT4 is a previously unidentified gene that maps to chromosome VII, between ADE6 and CLY8.
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    URL: http://dx.doi.org/10.1007/BF00279450
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    Characterization of the cyrl-2 UGA mutation in Saccharomyces cerevisiae (1993)
    Springer
    Molecular genetics and genomics 237 (1993), S. 463-466 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; cyrl-2 ; Nonsense mutation ; CAMP
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary cyrl-2 is a temperature-sensitive mutation of the yeast adenylate cyclase structural gene, CYR1. The cyrl-2 mutation has been suggested to be a UGA mutation since a UGA suppressor SUP201 has been isolated as a suppressor of the cyrl-2 mutation. Construction of chimeric genes restricted the region containing the cyrl-2 mutation, and the cyrl-2 UGA mutation was identified at codon 1282, which lies upstream of the region coding for the catalytic domain of adenylate cyclase. Alterations in the region upstream of the cyrl-2 mutation site result in null mutations. The complete open reading frame of the cyrl-2 gene expressed under the control of the GAL1 promoter complemented cyrl-dl in a galactose-dependent manner. These results suggest that at the permissive temperature weak readthrough occurs at the cyrl-2 mutation site to produce low levels of active adenylate cyclase. An endogenous suppressor in yeast cells is assumed to be responsible for this readthrough.
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    URL: http://dx.doi.org/10.1007/BF00279452
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    Characterization of the MKS1 gene, a new negative regulator of the Ras-cyclic AMP pathway in Saccharomyces cerevislae (1993)
    Springer
    Molecular genetics and genomics 238 (1993), S. 6-16 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; cAMP MKS1 ; GAL11
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In order to isolate genes that function downstream of the Ras-cAMP pathway in Saccharomyces cerevisiae, a YEp13-based genomic library was screened for clones that inhibit growth of cells with diminished A-kinase activity. One such gene, MKS1, was found to encode a hydrophilic 52 kDa protein that shares weak homology with the yeast SPT2/SIN1 gene product. Three lines of evidence suggest that the MKS1 gene product is a negative regulator downstream of the Ras-cAMP pathway: (i) overexpression of MKS1 inhibits growth of cyrl disruptant cells on YPD medium containing a low concentration of cAMP; (ii) overexpression of MKS1 does not affect TPK1 expression; and (iii) the temperature-sensitive cyrl-230 mutation is partially suppressed by mks1 disruption. The mks1 mutant shows similar phenotypes to gal11/spt13, i.e., it cannot grow on YPGal containing ethidium bromide at 25°C, or on YPGly or SGal at 37°C. The mks1 gal11 double mutant shows more marked phenotypic changes than the single mutants. These results suggest that MKS1 is involved in transcriptional regulation of several genes by cAMP.
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    URL: http://dx.doi.org/10.1007/BF00279524
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    Functional conservation between Schizosaccharomyces pombe ste8 and Saccharomyces cerevisiae STE11 protein kinases in yeast signal transduction (1992)
    Springer
    Molecular genetics and genomics 235 (1992), S. 122-130 
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    ISSN: 1617-4623
    Keywords: Schizosaccharomyces pombe ; Saccharomyces cerevisiae ; Signal transduction ; Sexual differentiation ; Protein kinase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In fission yeast (Schizosaccharomyces pombe), the mat1-Pm gene, which is required for entry into meiosis, is expressed in response to a pheromone signal. Cells carrying a mutation in the ste8 gene are unable to induce transcription of mat1-Pm in response to pheromone, suggesting that the ste8 gene product functions in the signal transduction pathway. The ste8 + gene encodes a 659 amino acid putative protein kinase, which is identical to the previously identified byr2 suppressor of the ras1 defect. Furthermore, ste8 + is highly homologous to the Saccharomyces cerevisiae STE11 gene, which functions in signal transduction in budding yeast. Expression of the S. cerevisiae STE11 gene in S. pombe ste8 mutants restores the ability to transcribe mat1-Pm in response to pheromone. Also, such cells become capable of conjugation and sporulation. When mat1-Pm is artifically expressed from a heterologous promoter, ste8 mutant cells will enter meiosis. This demonstrates that the meiotic defect of ste8 mutants is due to the absence of the mat1-Pm gene product.
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    URL: http://dx.doi.org/10.1007/BF00286189
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    The pso4-1 mutation reduces spontaneous mitotic gene conversion and reciprocal recombination in Saccharomyces cerevisiae (1992)
    Springer
    Molecular genetics and genomics 235 (1992), S. 311-316 
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    ISSN: 1617-4623
    Keywords: pso4-1 mutation ; Saccharomyces cerevisiae ; Mitotic recombination ; 8-Methoxypsoralen photoreaction ; his4 gene duplication
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Spontaneous mitotic recombination was examined in the haploid pso4-1 mutant of Saccharomyces cerevisiae and in the corresponding wild-type strain. Using a genetic system involving a duplication of the his4 gene it was shown that the pso4-1 mutation decreases at least fourfold the spontaneous rate of mitotic recombination. The frequency of spontaneous recombination was reduced tenfold in pso4-1 strains, as previously observed in the rad52-1 mutant. However, whereas the rad52-1 mutation specifically reduces gene conversion, the pso4-1 mutation reduces both gene conversion and reciprocal recombination. Induced mitotic recombination was also studied in pso4-1 mutant and wild-type strains after treatment with 8-methoxypsoralen plus UVA and 254 nm UV irradiation. Consistent with previous results, the pso4-1 mutation was found strongly to affect recombination induction.
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    URL: http://dx.doi.org/10.1007/BF00279375
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    A GCN4 protein recognition element is not sufficient for GCN4-dependent regulation of transcription in the ARO7 promoter of Saccharomyces cerevisiae (1990)
    Springer
    Molecular genetics and genomics 224 (1990), S. 57-64 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; AR07 gene ; Chorismate mutase ; GCN4 ; Transcriptional regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The gene AR07 encodes the monofunctional enzyme chorismate mutase, a branch point enzyme in the aromatic amino acid biosynthetic pathway in Saccharomyces cerevisiae. We investigated the transcription of the AR07 gene. Three 5′ ends at positions − 36, − 56 and − 73 and the 3′ end of the transcripts 146 bp downstream of the translational stop codon were mapped. As in the promoters of other aromatic amino acid biosynthetic genes, a recognition element for the GCN4 transcriptional activator of amino acid biosynthesis is located 425 base pairs (bp) upstream of the first transcriptional start point. This element binds GCN4 specifically in vitro. Northern analysis and determination of the specific enzyme activity reveals however, that the element is not sufficient to mediate transcriptional regulation by GCN4 in vivo. We thus suggest that in addition to a consensus sequence capable of binding the GCN4 protein other factors like, for example, chromatin structure, determine whether a recognition site for a transcription factor functions as an upstream activation sequence.
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    URL: http://dx.doi.org/10.1007/BF00259451
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    Budding yeast mutants showing constitutive basal levels of expression of DNA synthesis genes (1993)
    Springer
    Molecular genetics and genomics 240 (1993), S. 36-42 
    Details
    ISSN: 1617-4623
    Keywords: Yeast ; Saccharomyces cerevisiae ; DNA synthesis genes ; Cell cycle regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Two mutants have been isolated in Saccharomyces cerevisiae in which transcripts from at least CDC8, CDC9, CDC21 (TMP1) and POL1 genes are expressed constitutively in cells blocked at START by use of either α-pheromone or the cdc28 mutation. The transcripts from these genes also persist in mutant stationary phase cells; however, cell cycle regulation of these four DNA synthesis genes occurs normally in late G1. The mutation therefore does not appear to lie in the MCB-DSC1 (MBF) system that controls the periodic regulation of the genes, but must affect some control mechanism regulating basal levels of expression.
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    A yeast mutant, PRP20, altered in mRNA metabolism and maintenance of the nuclear structure, is defective in a gene homologous to the human gene RCC1 which is involved in the control of chromosome condensation (1990)
    Springer
    Molecular genetics and genomics 224 (1990), S. 72-80 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Splicing ; Nuclear structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We report on the characterization of the yeast prp20-1 mutant. In this temperature-sensitive mutant, multiple steps of mRNA metabolism are affected. The prp20-1 mutant strain showed alterations in mRNA steady-state levels, defective mRNA splicing and changes in transcription initiation or termination when shifted from the permissive to the non-permissive temperature. In addition, a change in the structure of the nucleus in these cells became apparent. Electron microscopy revealed an altered structure of the nucleoplasm of prp20-1 mutant cells when grown at the no-permissive temperature that was not observed in cells grown at the permissive temperature or in wild-type cells. The wild-type PRP20 gene was isolated and sequenced. The putative PRP20 protein has a molecular weight of 52 kDa. We found that the PRP20 gene is identical to the yeast SRM1 gene (Clark and Sprague 1989). In addition, the PRP20 protein sequence shows significant sequence similarity to the human RCC1 protein (Ohtsubo et al. 1987). This protein has been implicated in the control of chromosome condensation. Based on the phenotype of the prp20-1 mutant and the observed sequence similarity to the human RCC1 protein, we postulate that the yeast PRP20 protein is involved in the control of nuclear organization.
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    The MSS51 gene product is required for the translation of the COX1 mRNA in yeast mitochondria (1990)
    Springer
    Molecular genetics and genomics 224 (1990), S. 111-118 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Translation ; Splicing ; Paromomycin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The MSS51 gene product has been previously shown to be involved in the splicing of the mitochondrial pre-mRNA of cytochrome oxidase subunit I (COX1). We show here that it is specifically required for the translation of the COX1 mRNA. Furthermore, the paromomycin-resistance mutation (P inf454 supR ) which affects the 15 S mitoribosomal RNA, interferes, directly or indirectly, with the action of the MSS51 gene product. Possible roles of the MSS51 protein on the excision of COX1 introns are discussed.
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    Induction of “General Control” and thermotolerance in cdc mutants of Saccharomyces cerevisiae (1990)
    Springer
    Molecular genetics and genomics 224 (1990), S. 257-263 
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    ISSN: 1617-4623
    Keywords: General Control ; Thermotolerance ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In Saccharomyces cerevisiae starvation for a single amino acid activates the transcription of a set of genes belonging to different amino acid biosynthetic pathways (General Control, GC). We show that mutants affected in GC regulation are also affected in their response to thermal stress. Moreover, growth conditions that are known to induce heat shock proteins induce the GC response. However, unlike heat shock proteins, the transcriptional activator of GC, GCN4, is not induced after a short exposure to heat, and in gcn mutant strains induction of heat resistance is normal.
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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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    The synthesis of the two S-adenosyl-methionine synthetases is differently regulated in Saccharomyces cerevisiae (1991)
    Springer
    Molecular genetics and genomics 226 (1991), S. 224-232 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; SAM1 and SAM2 genes ; Transcription
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary S-adenosyl-l-methionine (AdoMet) is synthesized by transfer of the adenosyl moiety of ATP to the sulfur atom of methionine. This reaction is catalysed by AdoMet synthetase. In all eukaryotic organisms studied so far, multiple forms of AdoMet synthetases have been reported and from their recent study, it appears that AdoMet synthetase is an exceptionally well conserved enzyme through evolution. In Saccharomyces cerevisiae, we have demonstrated the existence of two AdoMet synthetases encoded by genes SAM1 and SAM2. Yeast, which is able to concentrate exogenously added AdoMet, is thus a particularly useful biological system to understand the role and the physiological significance of the preservation of two almost identical AdoMet synthetases. The analysis of the expression of the two SAM genes in different genetic backgrounds during growth under different conditions shows that the expression of SAM1 and SAM2 is regulated differently. The regulation of SAM1 expression is identical to that of other genes implicated in AdoMet metabolism, where as SAM2 shows a specific pattern of regulation. A careful analysis of the expression of the two genes and of the variations in the methionine and AdoMet intracellular pools during the growth of different strains lead us to postulate the existence of two different AdoMet pools, each one suppplied by a different AdoMet synthetase but in equilibrium with each other. This could be a means of storing AdoMet whenever this metabolite is overproduced, thus avoiding the degradation of a metabolite the synthesis of which is energetically expensive.
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    TheSaccharomyces cerevisiae genes (CMP1 andCMP2) encoding calmodulin-binding proteins homologous to the catalytic subunit of mammalian protein phosphatase 2B (1991)
    Springer
    Molecular genetics and genomics 227 (1991), S. 52-59 
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    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Calmodulin-binding protein ; Protein phosphatase (2B type) ; Calcineurin A
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Saccharomyces cerevisiae genomic clones that encode calmodulin-binding proteins were isolated by screening a λgt11 expression library using125I-labeled calmodulin as probe. Among the cloned yeast genes, we found two closely related genes (CMP1 andCMP2) that encode proteins homologous to the catalytic subunit of phosphoprotein phosphatase. The presumed CMP1 protein (62999 Da) and CMP2 protein (68496 Da) contain a 23 amino acid sequence very similar to those identified as calmodulin-binding sites in many calmodulin-regulated proteins. The yeast genes encode proteins especially homologous to the catalytic subunit of mammalian phosphoprotein phosphatase type 213 (calcineurin). The products of theCMP1 andCMP2 genes were identified by immunoblot analysis of cell extracts as proteins of 62000 and 64000 Da, respectively. Gene disruption experiments demonstrated that elimination of either or both of these genes had no effect on cell viability, indicating that these genes are not essential for normal cell growth.
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    URL: http://dx.doi.org/10.1007/BF00260706
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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 
    Details
    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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    URL: http://dx.doi.org/10.1007/BF00277347
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    The Escherichia coli recA gene increases resistance of the yeast Saccharomyces cerevisiae to ionizing and ultraviolet radiation (1991)
    Springer
    Molecular genetics and genomics 227 (1991), S. 473-480 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; recA gene expression ; Resistance to ionizing and ultraviolet radiation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The Escherichia coli recA protein coding region was ligated into an extrachromosomally replicating yeast expression vector downstream of the yeast alcohol dehydrogenase promoter region to produce plasmid pADHrecA. Transformation of the wild-type yeast strains YNN-27 and 7799-4B, as well as the recombination-deficient rad52-t C5-6 mutant, with this shuttle plasmid resulted in the expression of the bacterial 38 kDa RecA protein in exponential phase cells. The wild-type YNN27 and 7799-4B transformants expressing the bacterial recA gene showed increased resistance to the toxic effects of both ionizing and ultraviolet radiation. RecA moderately stimulated the UV-induced mutagenic response of 7799-4B cells. Transformation of the rad52-t mutant with plasmid pADHrecA did not result in the complementation of sensitivity to ionizing radiation. Thus, the RecA protein endows the yeast cells with additional activities, which were shown to be error-prone and dependent on the RAD52 gene.
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    URL: http://dx.doi.org/10.1007/BF00273940
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    Cloning and expression in yeast of a cDNA clone encoding Aspergillus oryzae neutral protease II, a unique metalloprotease (1991)
    Springer
    Molecular genetics and genomics 228 (1991), S. 97-103 
    Details
    ISSN: 1617-4623
    Keywords: Fungi ; Saccharomyces cerevisiae ; Zinc ; Processing ; Pro region
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The neutral protease II (NpII) from Aspergillus oryzae is a zinc-containing metalloprotease with some unique properties. To elucidate its structure, we isolated a full-length cDNA clone for NpII. Sequence analysis reveals that NpII has a prepro region consisting of 175 amino acids preceding the mature region, which consists of 177 amino acids. As compared with other microbial metalloproteases, NpII is found to be unique in that it shares only a limited homology with them around two zinc ligand His residues and that the positions of the other zinc ligand (Glu) and the active site (His) cannot be established by homology. When a plasmid designed to express the prepro NpII cDNA was introduced into Saccharomyces cerevisiae and the transformant was cultured in YPD medium (2% glucose, 2% polypeptone, 1% yeast extract), it secreted a proNpII. However, in a culture of the same medium containing 0.2 mM ZnCl2, it secreted a mature NpII with a specific activity and N-terminus identical to those of native NpII. This observation suggests that either an autoproteolytic activity or a yeast protease effected the processing.
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    URL: http://dx.doi.org/10.1007/BF00282453
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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 
    Details
    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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    URL: http://dx.doi.org/10.1007/BF00283426
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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 
    Details
    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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    URL: http://dx.doi.org/10.1007/BF00283425
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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 
    Details
    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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    URL: http://dx.doi.org/10.1007/BF00284206
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    The yeast RNA1 protein, necessary for RNA processing, is homologous to the human ribonuclease/angiogenin inhibitor (RAI) (1992)
    Springer
    Molecular genetics and genomics 233 (1992), S. 315-318 
    Details
    ISSN: 1617-4623
    Keywords: RNA1 ; Ribonuclease/angiogenin inhibitor ; Homology ; RNA metabolism ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutations in theRNA1 gene ofSaccharomyces cerevisiae, which encodes an essential cytosolic protein, affect the production and processing of all major classes of RNA. The mechanisms underlying these effects are not at all understood. Detailed comparative sequence analyses revealed that the RNA1 protein belongs to a superfamily, the members of which contain repetitive “leucine-rich motifs” (LRM). Within this superfamily RNA1 is most closely related to the ribonuclease/angiogenin inhibitor (RAI), which is a tightly binding inhibitor of ribonucleolytic activities in mammals. These results not only provide important clues to the structure, function and evolution of the RNAI protein, but also have intriguing implications for possible novel functions of RAI.
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    URL: http://dx.doi.org/10.1007/BF00587594
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    Alteration of an amino acid residue outside the active site of the ricin A chain reduces its toxicity towards yeast ribosomes (1991)
    Springer
    Molecular genetics and genomics 230 (1991), S. 81-90 
    Details
    ISSN: 1617-4623
    Keywords: Ricin ; Toxin ; Mutant ; Saccharomyces cerevisiae ; Expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Yeast transformants containing integrated copies of a galactose-regulated, ricin toxin A chain (RTA) expression plasmid were constructed and used in an attempt to isolate RTA-resistant yeast mutants. Analysis of RNA from mutant strains demonstrated that approximately half contained ribosomes that had been partially modified by RTA, although all the strains analysed transcribed full-length RTA RNA. The mutant strains could have mutations in yeast genes giving rise to RTA-resistant ribosomes or they could contain alterations within the RTA-encoding DNA causing production of mutant toxin. Ribosomes isolated from mutant strains were shown to be susceptible to RTA modification in vitro suggesting that the strains contain alterations in RTA. This paper describes the detailed analysis of one mutant strain which has a point mutation that changes serine 203 to asparagine in RTA protein. Although serine 203 lies outside the proposed active site of RTA its alteration leads to the production of RTA protein with a greatly reduced level of ribosome modifying activity. This decrease in activity apparently allows yeast cells to survive expression of RTA as only a proportion of the ribosomes become modified. We demonstrate that the mutant RTA preferentially modifies 26S rRNA in free 60S subunits and has lower catalytic activity compared with native RTA when produced in Escherichia coli. Such mutations provide a valuable means of identifying residues important in RTA catalysis and of further understanding the precise mechanism of action of RTA.
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    URL: http://dx.doi.org/10.1007/BF00290654
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    The two genes encoding protein synthesis initiation factor eIF-5A in Saccharomyces cerevisiae are members of a duplicated gene cluster (1992)
    Springer
    Molecular genetics and genomics 233 (1992), S. 487-490 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Translation ; Initiation factor ; Chromosomal mapping ; Pulsed-field electrophoresis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Translation initiation factor eIF-5A is an abundant protein in which a lysine residue is modified by spermidine to form the amino acid derivative, hypusine. The factor is encoded by two genes in Saccharomyces cerevisiae, called TIF51A and TIF51B, which are regulated reciprocally by oxygen and by heme. TIF51B, also called ANBI, is located on chromosome X in a region called COR. We physically mapped TIF51A and its associated serine tRNA2 gene by the method of chromosome fragmentation and pulsed-field gel electrophoresis. TIF5IA maps 90 kb from the left end of chromosome V in a region called ARC. The COR and ARC regions contain CYCI and CYC7, respectively, and appear to be duplications carrying numerous related genes. The arrangements of related genes in the two regions are incompatible with a duplication mechanism involving a circular intermediate.
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    URL: http://dx.doi.org/10.1007/BF00265449
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    Cloning, sequencing and characterization of the Saccharomyces cerevisiae URA7 gene encoding CTP synthetase (1991)
    Springer
    Molecular genetics and genomics 231 (1991), S. 7-16 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; CTP synthetase ; Pyrimidine pathway ; Intracellular pyrimidine pool ; Non-essential gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The URA7 gene of Saccharomyces cerevisiae encodes CTP synthetase (EC 6.3.4.2) which catalyses the conversion of uridine 5′-triphosphate to cytidine 5′-triphosphate, the last step of the pyrimidine biosynthetic pathway. We have cloned and sequenced the URA 7 gene. The coding region is 1710 by long and the deduced protein sequence shows a strong degree of homology with bacterial and human CTP synthetases. Gene disruption shows that URA7 is not an essential gene: the level of the intracellular CTP pool is roughly the same in the deleted and the wild-type strains, suggesting that an alternative pathway for CTP synthesis exists in yeast. This could involve either a divergent duplicated gene or a different route beginning with the amination of uridine mono- or diphosphate.
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    URL: http://dx.doi.org/10.1007/BF00293815
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    The UGA3 gene regulating the GABA catabolic pathway in Saccharomyces cerevisiae codes for a putative zinc-finger protein acting on RNA amount (1990)
    Springer
    Molecular genetics and genomics 220 (1990), S. 269-276 
    Details
    ISSN: 1617-4623
    Keywords: GABA ; Saccharomyces cerevisiae ; Transcription ; DNA sequence ; Zinc finger
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The UGA3 gene of Saccharomyces cerevisiae is required for 4-aminobutyric acid (GABA)-dependent induction of the UGA1, UGA2 and UGA4 genes which encode the two GABA catabolic enzymes and a GABA-specific permease, respectively. Measurements of UGA1-specific transcripts show that induction of UGA1 correlates with accumulation of its RNA and requires a functional UGA3 gene. A 2 kb DNA fragment complementing the uga3 mutation was isolated and shown to contain the UGA3 gene. The primary structure of the UGA3 encoded protein was deduced from the DNA sequence, and contains an N-terminal, cysteine-rich motif similar in sequence to regions found in other fungal regulatory proteins and which are supposed to form zinc finger structures involved in DNA binding. Mutations were identified in the UGA3 genes isolated from uninducible and constitutive uga3 alleles. One case of intragenic complementation between two uninducible uga3 mutants is reported, indicating a possible oligomeric structure for UGA3. The role of UGA3 is discussed in relation to its genetic properties and its predicted structure.
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    URL: http://dx.doi.org/10.1007/BF00260493
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    Regulation of chorismate mutase in Saccharomyces cerevisiae (1990)
    Springer
    Molecular genetics and genomics 220 (1990), S. 283-288 
    Details
    ISSN: 1617-4623
    Keywords: Chorismate mutase ; Saccharomyces cerevisiae ; Repression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The Saccharomyces cerevisiae ARO7 gene was cloned by screening a wild-type gene bank for complementation of an aro7 auxotrophic mutant. In vitro mutagenesis of the isolated plasmid (pJFB1) gave several transformants resistant to levels of the phenylalanine analogue 2-thienylalanine inhibitory to the wild-type transformant. Chorismate mutase assays indicated that two of the mutants (J14-26IV6 and J14-26IV9) were resistant to feedback inhibition by tyrosine displayed by wild-type strains. Analysis of the effect of other aromatic amino acids on chorismate mutase activity showed that tryptophan counteracted this inhibition. Analysis of the effect of tyrosine in the growth medium on enzyme activity indicated that the wild-type ARO7 gene was repressed by tyrosine, a phenomenon not previously reported. Two of the 2-thienylalanine resistant mutants (J14-26IV3 and J14-26IV9) appeared to be resistant to this repression. Transcriptional analysis confirmed that the level of ARO7 transcript decreased with increasing tyrosine concentration. In stain J14-26IV9 the ARO7 transcript level was not affected. J14-26IV9, therefore, appears to be a double mutant, resistant to both feedback inhibition and repression by tyrosine.
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    URL: http://dx.doi.org/10.1007/BF00260495
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    Dual function of a new nuclear gene for oxidative phosphorylation and vegetative growth in yeast (1992)
    Springer
    Molecular genetics and genomics 232 (1992), S. 58-64 
    Details
    ISSN: 1617-4623
    Keywords: Essential gene ; Respiration ; Mutants ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A new gene essential for cell viability and indispensable for the biogenesis of a functional respiratory chain in Saccharomyces cerevisiae was isolated by complementing a temperature-sensitive mutant. This conditional nuclear mutation selectively affects oxidative phosphorylation at restrictive temperatures. At the molecular level a severe and complex defect inside mitochondria is observed, with drastically reduced levels of mitochondrial transcripts. Surprisingly a null mutation in this nuclear gene in a haploid yeast strain leads to cell death. Spores containing a disrupted copy of the gene exhibit a severe growth defect and cell division stops irreversibly after 3 to 4 days. It is shown that the null and conditional mutants are indeed allelic. This finding demonstrates a dual function of the gene product in oxidative phosphorylation and vegetative growth. The putative protein product, as deduced from the sequence of the relevant reading frame is characterized by a low molecular weight of approximately 14 kDa, a high content of charged amino acids and a very low codon bias index. A transcript of low abundance and with a length of about 600 nucleotides can be assigned to this gene.
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    URL: http://dx.doi.org/10.1007/BF00299137
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    Regulation of the yeast RAD2 gene DNA damage-dependent induction correlates with protein binding to regulatory sequences and their deletion influences survival (1992)
    Springer
    Molecular genetics and genomics 232 (1992), S. 247-256 
    Details
    ISSN: 1617-4623
    Keywords: DNA damage ; Excision repair ; Saccharomyces cerevisiae ; Gene regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In the yeast Saccharomyces cerevisiae the RAD2 gene is absolutely required for damage-specific incision of DNA during nucleotide excision repair and is inducible by DNA-damaging agents. In the present study we correlated sensitivity to killing by DNA-damaging agents with the deletion of previously defined specific promoter elements. Deletion of the element DRE2 increased the UV sensitivity of cells in both the G1/early S and S/G2 phases of the cell cycle as well as in stationary phase. On the other hand, increased UV sensitivity associated with deletion of the sequence-related element DRE1 was restricted to cells irradiated in G1/S. Specific binding of protein(s) to the promoter elements DRE1 and DRE2 was observed under non-inducing conditions using gel retardation assays. Exposure of cells to DNA-damaging agents resulted in increased protein binding that was dependent on de novo protein synthesis.
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    URL: http://dx.doi.org/10.1007/BF00280003
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    Expression of yeast cytochrome C1 is controlled at the transcriptional level by glucose, oxygen and haem (1992)
    Springer
    Molecular genetics and genomics 232 (1992), S. 447-459 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Cytochrome c 1 ; Promoter dissection ; HAP1, HAP2 transcription factors ; Centromere and promoter-binding factor (CPF1)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The nuclear gene for cytochrome c 1 in Saccharomyces cerevisiae (CYT1) was localized on chromosome XV. Its upstream region was identified by functional complementation. Fusion to the lacZ reporter gene on a CEN plasmid allowed study of the effect of carbon sources and of specific deletion mutations on expression of the gene in yeast transformants. Detailed promoter analysis combined with expression studies in recipient strains defective in regulatory genes identified cis-acting sites and transcription factors involved in the regulated expression of the cytochrome c 1 gene. These analyses showed that, in the presence of glucose, transcription of CYT1 is positively controlled by oxygen, presumably through the haem signal, and mediated by the HAP1-encoded transactivator. It is additionally regulated by the HAP2/3/4 complex which mediates gene activation mainly under glucose-free conditions. Basal transcription is, in part, effected by CPF1, a centromere and promoter-binding factor.
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    URL: http://dx.doi.org/10.1007/BF00266250
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    TheNAM8 gene inSaccharomyces cerevisiae encodes a protein with putative RNA binding motifs and acts as a suppressor of mitochondrial splicing deficiencies when overexpressed (1992)
    Springer
    Molecular genetics and genomics 233 (1992), S. 136-144 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Nuclear gene ; Mitochondrial splicing ; Suppression ; RNA binding proteins
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have characterized the nuclear geneNAM8 inSaccharomyces cerevisiae. It acts as a suppressor of mitochondrial splicing deficiencies when present on a multicopy plasmid. The suppressed mutations affect RNA folding and are located in both group I and group II introns. The gene is weakly transcribed in wildtype strains, its overexpression is a prerequisite for the suppressor action. Inactivation of theNAM8 gene does not affect cell viability, mitochondrial function or mitochondrial genome stability. TheNAM8 gene encodes a protein of 523 amino acids which includes two conserved (RNP) motifs common to RNA-binding proteins from widely different organisms. This homology with RNA-binding proteins, together with the intronic location of the suppressed mitochondrial mutations, suggests that the NAM8 protein could be a non-essential component of the mitochondrial splicing machinery and, when present in increased amounts, it could convert a deficient intron RNA folding pattern into a productive one.
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    URL: http://dx.doi.org/10.1007/BF00587571
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    Differential regulation of STA genes of Saccharomyces cerevisiae (1990)
    Springer
    Molecular genetics and genomics 222 (1990), S. 87-96 
    Details
    ISSN: 1617-4623
    Keywords: Glucoamylase ; Sporulation ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae var. diastaticus ; STA genes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The single glucoamylase gene (SGA1) of the yeast Saccharomyces cerevisiae is expressed exclusively during the sporulation phase of the life cycle. Enzymatic studies and nucleic acid sequence comparisons have shown that the SGA1 glucoamylase is closely related to the secreted enzymes of S. cerevisiae var. diastaticus. The latter are encoded by any of three unlinked STA genes, which have been proposed to derive from the ancestral SGA1 form by genomic rearrangement. We show that the regulation of SGA1 is distinct from that of the other members of the STA gene family. SGA1 expression did not respond to STA10, the primary determinant of glucoamylase expression from STA2. Unlike STA2, SGA1 was not regulated directly by the mating type locus. Expression of SGA1 depended on the function of the MAT products in supporting sporulation and not on the formation of haploid progeny spores or on the composition of the mating type locus per se. We conclude that the STA genes acquired regulation by STA10 and MAT by the genomic rearrangements that led to their formation. This regulation is thus distinct from that of the ancestral SGA1 gene.
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    URL: http://dx.doi.org/10.1007/BF00283028
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    Molecular basis for determining the sensitivity of eucaryotes to the antimitotic drug rhizoxin (1990)
    Springer
    Molecular genetics and genomics 222 (1990), S. 169-175 
    Details
    ISSN: 1617-4623
    Keywords: Aspergillus nidulans ; Schizosaccharomyces pombe ; Saccharomyces cerevisiae ; Drug resistance ; β-tubulin mutation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Rhizoxin, an antibiotic, exhibits potent anti-mitotic activity against most eucaryotic cells including those of higher vertebrates, plants and fungi by binding to β-tubulin. ThebenA gene of three independently isolated rhizoxin-resistant (Rhir) mutants ofAspergillus nidulans was cloned, sequenced and compared with that of the wild-type, rhizoxin-sensitive (Rhis) strain. In all three Rhir mutants, the AAC codon for Asn-100 of thebenA β-tubulin gene was altered to ATC, coding for Ile. Sequence displacement experiments confirmed that the substitution of Ile for Asn-100 confers resistance to rhizoxin in this organism. The amino acid sequences of β-tubulin surrounding the 100th amino acid residue from the N-terminus including Asn-100 are highly conserved with a few exceptions. The fission yeastSchizosaccharomyces pombe and the budding yeastSaccharomyces cerevisiae are naturally occurring Rhir organisms whose β-tubulin genes encode Ile and Val respectively at the 100th amino acid residue. The Ile-100 ofS. pombe and the Val-100 ofS. cerevisiae were altered to Asn using site-directed mutagenesis and gene displacement techniques. The resultant haploid strains of these two yeasts uniquely expressing β-tubulin (Asn-100) instead of β-tubulin (Ile-100 or Val-100) were found to be Rhis. Haploid yeast expressing β-tubulin (Asn-100) is normal except for its sensitivity to rhizoxin. These results suggest that rhizoxin resistance has a common basis in both naturally occurring species and experimentally selected mutants in the substitution of Ile or Val for Asn-100 in β-tubulin.
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    URL: http://dx.doi.org/10.1007/BF00633814
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    Correct splicing of modified introns of a Rhizopus proteinase gene in Saccharomyces cerevisiae (1990)
    Springer
    Molecular genetics and genomics 223 (1990), S. 11-16 
    Details
    ISSN: 1617-4623
    Keywords: Rhizopus aspartic proteinase ; Splicing of intron ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The intron of the Rhizopus aspartic proteinase gene (RNAP-I) was modified by in vitro mutagenesis and examined for its splicing efficiency in Saccharomyces cerevisiae. The wild-type intron of the RNAP-I gene was not spliced at all in spite of its structural similarity to introns of S. cerevisiae. The primary transcript of the RNAP-I gene was converted to correctly translatable mRNA only when the complete consensus sequence of S. cerevisiae introns (i.e. 5″-GTATGT-----TACTAAC-----TAG-3″) was introduced into its intron, although the efficiency of splicing was low. It is also shown that transformants carrying the RNAP-I gene with the complete consensus sequence of S. cerevisiae introns produce active RNAP-I protein.
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    URL: http://dx.doi.org/10.1007/BF00315791
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    Expression in Saccharomyces cerevisiae of a gene associated with cytoplasmic male sterility from maize: Respiratory dysfunction and uncoupling of yeast mitochondria (1990)
    Springer
    Molecular genetics and genomics 223 (1990), S. 24-32 
    Details
    ISSN: 1617-4623
    Keywords: Cochliobolus heterostrophus race T disease ; Maize cytoplasmic male sterility ; Mitochondria ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We asked whether the mitochondrial T-urf13 gene, associated with the male sterility phenotype of T cytoplasm in maize, can be expressed in Saccharomyces cerevisiae and whether this expression can mimic the effects observed in maize. We introduced the universal code equivalent of the T-urf13 gene into the S. cerevisiae nucleus by transformation and directed its translation product into mitochondria by means of a fusion with the targeting presequence from Neurospora crassa ATPase subunit 9. We show that expression of the universal code equivalent of the T-urf13 gene in the yeast nucleus does indeed mimic its effects in maize: respiratory growth of yeast is inhibited, respiration-deficient cytoplasmic mutants accumulate and NADH oxidation of isolated mitochondria is uncoupled. All these effects are observed only if the mitochondrial targeting peptide and methomyl or HmT toxin are present.
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    URL: http://dx.doi.org/10.1007/BF00315793
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    Deletion analysis of domain independence in the TRP1 gene product of Neurospora crassa (1990)
    Springer
    Molecular genetics and genomics 223 (1990), S. 49-57 
    Details
    ISSN: 1617-4623
    Keywords: Neurospora crassa ; Heterologous gene expression ; Saccharomyces cerevisiae ; Domain independence ; TRP1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The trifunctional TRP1 gene from Neurospora crassa (N-TRP1) was subcloned into the yeast-Escherichia coli shuttle vector YEp13 and expressed in Saccharomyces cerevisiae. The three activities of the N-TRP1 gene product were detected in yeast mutants that lacked either N-(5′-phosphoribosyl) anthranilate (PRA) isomerase or both the glutamine amidotransferase function of anthranilate synthase and indole-3-glycerol phosphate (InGP) synthase. The protein was detected on immunoblots only as the full length 83 kda product indicating that the trifunctional gene product was expressed in yeast primarily in a fully active, undegraded form. By placing the subcloned N-TRP1 gene under the control of the inducible PHO5 promoter from yeast, the expression of all three activities was increased to more than ten fold that of wild-type yeast and the overproduced protein could be visualized by SDS-polyacrylamide gel electrophoresis of crude extract and Coomassie Blue staining. Using the expression system described the effect of selective deletion of regions of the coding sequence of the N-TRP1 gene on expression of the three activities was tested. Expression of either the F- or C-domains, catalyzing respectively the PRA isomerase or InGP synthase activities, did not depend on the presence of the other domain in the active polypeptide. Furthermore, normal dimer formation occurred with a protein active for InGP synthase in a deletion derivative lacking most of the PRA isomerase domain, ruling out the hypothesis that interaction between the active site regions for PRA isomerase and InGP synthase accounted for dimer formation in the trifunctional product.
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    URL: http://dx.doi.org/10.1007/BF00315796
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    HSP12, a new small heat shock gene of Saccharomyces cerevisiae: Analysis of structure, regulation and function (1990)
    Springer
    Molecular genetics and genomics 223 (1990), S. 97-106 
    Details
    ISSN: 1617-4623
    Keywords: Heat shock ; Saccharomyces cerevisiae ; Stationary phase ; cAMP ; Thermotolerance
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have isolated a new small heat shock gene, HSP12, from Saccharomyces cerevisiae. It encodes a polypeptide of predicted Mr 12 kDa, with structural similarity to other small heat shock proteins. HSP12 gene expression is induced several hundred-fold by heat shock and on entry into stationary phase. HSP12 mRNA is undetectable during exponential growth in rich medium, but low levels are present when cells are grown in minimal medium. Analysis of HSP12 expression in mutants affected in cAMP-dependent protein phosphorylation suggests that the gene is regulated by cAMP as well as heat shock. A disruption of the HSP12 coding region results in the loss of an abundant 14.4 kDa protein present in heat shocked and stationary phase cells. It also leads to the induction of the heat shock response under conditions normally associated with low-level HSP12 expression. The HSP12 disruption has no observable effect on growth at various temperatures, nor on the ability to acquire thermotolerance.
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    URL: http://dx.doi.org/10.1007/BF00315801
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    MSl3, a multicopy suppressor of mutants hyperactivated in the RAS-CAMP pathway, encodes a novel HSP70 protein of Saccharomyces cerevisiae (1993)
    Springer
    Molecular genetics and genomics 240 (1993), S. 323-332 
    Details
    ISSN: 1617-4623
    Keywords: Heat shock response ; HSP70 ; Saccharomyces cerevisiae ; RAS-CAMP pathway ; Multicopy suppressor of ira1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: abstract The MSI3 gene was isolated as a multicopy suppressor of the heat shock-sensitive phenotype of the iral mutation, which causes hyperactivation of the RAS-cAMP pathway. Overexpression of MSI3 also suppresses the heat shock-sensitive phenotype of the bcyl mutant. Determination of the DNA sequence of MSI3 revealed that MSI3 can encode a 77.4 kDa protein related to the HSP70 family. The amino acid sequence of Msi3p is about 30% identical to that of the Ssalp of Saccharomyces cerevisiae. This contrasts with the finding that members of the HSP70 family generally show at least 50% amino acid identity. The consensus nucleotide sequence of the heat shock element (HSE) was found in the upstream region of MSI3. Moreover, the steady-state levels of the MSI3 mRNA and protein were increased upon heat shock. These results indicate that the MSI3 gene encodes a novel HSP70-like heat shock protein. Disruption of the MSI3 gene was associated with a temperature sensitive growth phenotype but unexpectedly, thermotolerance was enhanced in the disruptant.
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    URL: http://dx.doi.org/10.1007/BF00280382
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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 
    Details
    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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    URL: http://dx.doi.org/10.1007/BF00282757
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    Characterisation of PDC2, a gene necessary for high level expression of pyruvate decarboxylase structural genes in Saccharomyces cerevlsiae (1993)
    Springer
    Molecular genetics and genomics 241 (1993), S. 657-666 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Pyruvate decarboxylase ; Transcription ; Glucose induction ; Autoregulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The regulatory gene PDC2 was identified in a screen for mutations affecting pyruvate decarboxylase activity in yeast. I have cloned and sequenced this gene. The predicted protein of 925 amino acids has no homology to any sequence in the databases. However, the protein sequence is rich in asparagine and serine residues, as is often found for transcriptional regulators. The PDC2 deletion mutant exhibits a phenotype very similar to, but more severe than that of the point mutant: a strongly reduced pyruvate decarboxylase specific activity, slow, respiration-dependent growth on glucose, and accumulation of pyruvate. The activity of other glycolytic enzymes seems to be unaffected by the pdc2Δ mutation. Synthesis of pyruvate decarboxylase is regulated by PDC2 at the transcriptional level. Expression of the major structural gene for pyruvate decarboxylase, PDC1, is strongly reduced in pdc2Δ mutants. Transcription of the generally more weakly expressed PDC5 gene appears to be entirely abolished. However, glucose induction of pyruvate decarboxylase synthesis is unaffected. Thus, PDC2 is either important for a high basal level of PDC gene expression or it plays a positive role in the autoregulation that controls expression of PDC1 and PDC5.
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    URL: http://dx.doi.org/10.1007/BF00279908
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    Co-regulation with genes of phospholipid biosynthesis of the CTR/HNM1-encoded choline/nitrogen mustard permease in Saccbaromyces cerevisiae (1993)
    Springer
    Molecular genetics and genomics 241 (1993), S. 680-684 
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    ISSN: 1617-4623
    Keywords: Nitrogen mustard resistance ; Regulation of choline permease ; Co-regulation ; Phospholipid biosynthesis ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract An 815 by region of the promoter of the Saccharomyces cerevisiae gene CTR/HNM1, encoding choline permease was sequenced and its regulatory function analysed by deletion studies in an in-frame promoter-lacZ construct. In addition to the TATA box, a 10 by motif (consensus 5′-CATGTGAAAT-3′) was found to be mandatory for CTR/HNM1 expression. This ‘decamer’ motif is located between nucleotides −262 and −271 and is identical in 9 of 10 by with the regulatory motif found in the S. cerevisiae INO1 and CHO1 genes. Constructs with the 10 by sequence show high constitutive expression, while elimination or alterations at three nucleotide positions, of the decamer motif in the context of an otherwise unchanged promoter leads to total loss of β-galactosidase production. Expression of the CTR/HNM1 gene in wild-type cells is regulated by the phospholipid precursors inositol and choline; no such influence is seen in cells bearing mutations in the phospholipid regulatory genes INO2, INO4, and OPI1. There is no regulation by INO2 and OPI1 in the absence of the decamer motif. However constructs not containing this sequence (promoter intact to positions −213 or −152) are still controlled by INO4. Other substrates of the choline permease, i.e. ethanolamine, nitrogen mustard and nitrogen half mustard do not regulate expression of CTR/HNM1.
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    APMR2 tandem repeat with a modified C-terminus is located downstream from theKRS1 gene encoding lysyl-tRNA synthetase inSaccharomyces cerevisiae (1991)
    Springer
    Molecular genetics and genomics 227 (1991), S. 149-154 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Lysyl-tRNA synthetase ; PMR2 repeat ; Genome organization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary TheKRS1 gene encodes the cytoplasmic form ofSaccharomyces cerevisiae lysyl-tRNA synthetase. TheKRS1 locus has been characterized. The lysyl-tRNA synthetase gene is unique in the yeast genome. The gene is located on the right arm of chromosome IV and disruption of the open reading frame leads to lethality. These results contrast with the situation encountered inEscherichia coli where lysyl-tRNA synthetase is coded by two distinct genes,lysS andlysU, and further address the possible biological significance of this gene duplication. The nucleotide sequence of the 3′-flanking region has been established. It encodes a long open reading frame whose nucleotide and amino acid structures are almost identical toPMR2, a cluster of tandemly repeated genes coding for P-type ion pumps. The sequence alterations relative toPMR2 are mainly located at the C-terminus of the protein.
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    URL: http://dx.doi.org/10.1007/BF00260720
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    Analysis of yeast prp20 mutations and functional complementation by the human homologue RCC1, a protein involved in the control of chromosome condensation (1991)
    Springer
    Molecular genetics and genomics 227 (1991), S. 417-423 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; mRNA metabolism ; Nucleus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Mutations in the PRP20 gene of yeast show a pleiotropic phenotype, in which both mRNA metabolism and nuclear structure are affected. srm1 mutants, defective in the same gene, influence the signal transduction pathway for the pheromone response. The yeast PRP20/SRM1 protein is highly homologous to the RCC1 protein of man, hamster and frog. In mammalian cells, this protein is a negative regulator for initiation of chromosome condensation. We report the analysis of two, independently isolated, recessive temperature-sensitive prp20 mutants. They have identical G to A transitions, leading to the alteration of a highly conserved glycine residue to glutamic acid. By immunofluorescence microscopy the PRP20 protein was localized in the nucleus. Expression of the RCC1 protein can complement the temperature-sensitive phenotype of prp20 mutants, demonstrating the functional similarity of the yeast and mammalian proteins.
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    URL: http://dx.doi.org/10.1007/BF00273932
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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 
    Details
    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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    URL: http://dx.doi.org/10.1007/BF00281793
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    Temperature-sensitive mutants of hsp82 of the budding yeast Saccharomyces cerevisiae (1994)
    Springer
    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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    URL: http://dx.doi.org/10.1007/BF00285275
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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 
    Details
    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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    URL: http://dx.doi.org/10.1007/BF00283417
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    Mitochondrial dysfunction in yeast expressing the cytoplasmic male sterility T-urf13 gene from maize: analysis at the population and individual cell level (1993)
    Springer
    Molecular genetics and genomics 236 (1993), S. 299-308 
    Details
    ISSN: 1617-4623
    Keywords: Texas maize cytoplasmic male sterility ; Saccharomyces cerevisiae ; Mitochondria ; Image and flow cytometry ; 3,3′-Dihexyloxacarbocyanine iodide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The urf13TW gene, which is derived from the mitochondrial T-urf13 gene responsible for Texas cytoplasmic male sterility in maize, was expressed in Saccharomyces cerevisiae by targeting its translation product into mitochondria. Analysis by oxygraphy at the population level revealed that in the presence of methomyl the oxygen uptake of intact yeast cells carrying the targeted protein is strongly stimulated only with ethanol as respiratory substrate and not with glycerol, lactate, pyruvate, or acetate. When malate is the substrate oxidized by isolated mitochondria, interaction between the targeted protein and methomyl results in significant inhibition of oxygen uptake. This inhibition is eliminated and oxygen uptake is stimulated by subsequent addition of NAD+. Using 3,3′-dihexyloxacarbocyanine iodide [DiOC6(3)] as probe, interactive laser scanning and flow cytometry, which permit analysis at the individual cell level, demonstrated that specific staining of the mitochondrial compartment is obtained and that DiOC6(3) fluorescence serves as a measure of the membrane potential. Finally, it was shown that, as in T cytoplasm maize mitochondria, HmT toxin and methomyl dissipate the membrane potential of yeast mitochondria that carry the foreign protein. Furthermore, the results suggest that the HmT toxin and methomyl response is related to the plasmid copy number per cell and that the deleterious effect induced by HmT toxin is stronger than that of methomyl.
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    A point mutation in the core subunit gene of yeast mitochondrial RNA polymerase is suppressed by a high level of specificity factor MTF1 (1993)
    Springer
    Molecular genetics and genomics 237 (1993), S. 49-57 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Nuclear pet mutants ; Mitochondrial transcription ; Mutant RNA polymerase ; Specificity factor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The temperature-sensitive yeast mutant pet-ts798 is characterized by an altered mitochondrial transcription apparatus. The mutation has previously been shown to map in the RP041 gene encoding the core enzyme of mitochondrial RNA polymerase. In the present study the rpo41/pet-ts798 allele was cloned and sequenced, demonstrating that the mutant phenotype is caused by a single amino acid change in a conserved region of the core polymerase. The nuclear gene MTF1, previously isolated as a high copy suppressor of mutant rpo41/pet-ts798, and its gene product were characterized in more detail. Import of a MTF1-COXIV fusion protein in vivo and also import studies with in vitro synthesized MTF1 precursors indicate that MTF1 is a mitochondrial protein and that no apparent cleavage occurs during its import into mitochondria. DNA-binding assays demonstrate that the MTF1 protein alone interacts with DNA in a non-specific manner. An antibody directed against specificity factor MTF1 was raised and used for immunological quantification experiments. The results indicate that suppression is mediated by an increased level of MTF1 protein in mitochondria of the rpo41/pet-ts798 mutant. Possible implications of this finding for the mechanism of suppression are discussed.
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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)
    Springer
    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)
    Springer
    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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    URL: http://dx.doi.org/10.1007/BF00279755
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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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    URL: http://dx.doi.org/10.1007/BF00297275
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    Repair of 8-methoxypsoralen photoinduced cross-links in yeast (1991)
    Springer
    Molecular genetics and genomics 228 (1991), S. 335-344 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; DNA interstrand cross-links ; DNA repair ; Electron microscopy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The repair of interstrand cross-links induced by 8-methoxypsoralen plus UVA (365 nm) radiation DNA was analyzed in diploid strains of the yeast Saccharomyces cerevisiae. The strains employed were the wild-type D7 and derivatives homozygous for the rad18-1 or the rad3-12 mutation. Alkaline step-elution and electron microscopy were performed to follow the process of induction and removal of photoinduced crosslinks. In accordance with previous reports, the D7 rad3-12 strain failed to remove the induced lesions and could not incise cross-links. The strain D7 rad18-1 was nearly as efficient in the removal of 8-MOP photoadducts after 2 h of post-treatment incubation as the D7 RAD+ wild-type strain. However, as demonstrated by alkaline step-elution and electron microscopic analysis, the first incision step at DNA cross-links was three times more effective in D7 rad18-1 than in D7 RAD+. This is consistent with the hypothesis that the RAD18 gene product is involved in the filling of gaps resulting from persistent non-informational DNA lesions generated by the endonucleolytic processing of DNA cross-links. Absence of this gene product may lead to extensive strand breakage and decreased recognition of such lesions by structural repair systems.
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    URL: http://dx.doi.org/10.1007/BF00260625
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    The Saccharomyces cerevisiae SPT14 gene is essential for normal expression of the yeast transposon, Ty, as well as for expression of the HIS4 gene and several genes in the mating pathway (1991)
    Springer
    Molecular genetics and genomics 230 (1991), S. 310-320 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Ty ; Transcriptional activation ; SPT13/GAL11 ; SPT14
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary To investigate the role of the trans-acting transcription factor encoded by the essential SPT14 (SPT=Suppressor of Ty insertion mutations) gene, we have cloned, mapped and sequenced the gene. From the analysis of the effect of spt14 mutations on expression of various genes, we conclude that the SPT14 product has an important role in activation of Ty transcription as well as in the regulation of other genes including HIS4 and several of the a- and α-specific mating type genes. Similarities in the phenotypes of spt14 and spt13 mutants (suppression of Ty insertion mutations but not δ insertion mutations), lead to the suggestion that the SPT14 gene and the previously characterized SPT13/GAL11 gene might encode transcriptional regulators with related functions. Our current findings show that in contrast to SPT13/GAL11, which appears negatively to regulate Ty transcription, SPT14 plays a role in the activation of Ty transcription. Thus, despite the similarities in the suppression phenotype exhibited by spt13 and spt14 mutants, SPT13/GAL11 and SPT14 probably differ in their transcriptional roles.
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    URL: http://dx.doi.org/10.1007/BF00290682
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    The role of promoter elements of a ribosomal protein gene in Saccharomyces cerevisiae under various physiological conditions (1992)
    Springer
    Molecular genetics and genomics 234 (1992), S. 22-32 
    Details
    ISSN: 1617-4623
    Keywords: cis-acting elements ; Saccharomyces cerevisiae ; Transcriptional regulation ; Ribosomal protein genes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Previous work in our laboratory has shown that the 5′ nontranscribed promoter region of the gene for ribosomal protein (rp) S16A-1 of Saccharomyces cerevisiae, when fused to a lacZ gene, is necessary and sufficient to cause an increase in expression of the heterologous lacZ gene fusion product after cells have been shifted from a glycerol to glucose carbon source. This increase in expression is characteristic of that observed with the native rp gene. We have sought to define more precisely those areas of the promoter that may be involved in the differential expression/regulation of RPS16A-1 when host cells are subjected to a variety of nutritional environments. It has already been demonstrated by others that the promoter regions of most rp genes contain at least one consensus element, designated UASrpg, which is necessary for the transcriptional activation and maintenance of expression of the gene during steady-state growth in rich media. Our main experimental approach has been to create a series of 5′ end deletions in the promoter region of RPS16A-1. The individual truncated promoter fragments were then ligated to a lacZ fusion reporter construct. By assaying the cells for production of β-galactosidase and determining the abundance of lacZ mRNA, we have been able to determined the extent of fusion product expression. We assayed cells under three physiological conditions: steady-state growth in glucose, steady-state growth in glycerol and during sporulation. We report four main findings of our work.
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    URL: http://dx.doi.org/10.1007/BF00272341
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    NPK1, a nonessential protein kinase gene in Saccharomyces cerevisiae with similarity to Aspergillus nidulans nimA (1992)
    Springer
    Molecular genetics and genomics 234 (1992), S. 164-167 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Protein kinase ; Nonessential gene
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A new protein kinase gene [called NPKI (for nonessential protein kinase)] has been found on chromosome I of Saccharomyces cerevisiae between CDC15 and ADE1. The 435 amino acid/48 kDa gene product is very similar to known protein kinases. It is most closely related to the nimA protein of Aspergillus nidulans, displaying 45.9% identity and 63.5% similarity in the protein kinase domain. A 1.4 kb transcript of the NPKI gene was detected. Disruption of the NPKI gene impedes neither growth on glucose or a variety of other carbon sources, nor mating or sporulation.
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    URL: http://dx.doi.org/10.1007/BF00272358
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    ore2, a mutation affecting proline biosynthesis in the yeast Saccharomyces cerevisiae, leads to a cdc phenotype (1992)
    Springer
    Molecular genetics and genomics 234 (1992), S. 193-200 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Cell cycle ; Proline ; DNA sequencing
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We report here the isolation of temperature-sensitive mutants of the yeast Saccharomyces cerevisiae which exhibit cdc phenotypes. The recessive mutations defined four complementation groups, named ore1, ore2, ore3 and ore4. At the non-permissive temperature, strains bearing these mutations arrested in the G1 phase of the cell cycle. The wild-type allele of the gene altered in ore2 mutants was cloned. The nucleotide sequence of a fragment which can complement the mutation showed the presence of an open reading frame capable of encoding a protein with 286 amino acid residues. The deduced amino acid sequence showed 25% identity with that of the Escherichia coli Δ1-pyrroline-5-carboxylate reductase, an enzyme of the pathway for the biosynthesis of proline. The ore2 mutants, correspondingly, were found to be capable of growing at the non-permissive temperature on a synthetic medium supplemented with proline. In addition, the chromosomal location of the gene and its restriction map were compatible with those previously reported for the PRO3 gene which encodes the S. cerevisiae Δ1-pyrroline-5-carboxylate reductase.
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    URL: http://dx.doi.org/10.1007/BF00283839
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    Positive regulation of the LPD1 gene of Saccharomyces cerevisine by the HAP2/HAP3/HAP4 activation system (1992)
    Springer
    Molecular genetics and genomics 231 (1992), S. 296-303 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Lipoamide dehydrogenase ; HAP activation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The LPD1 gene of Saccharomyces cerevisiae, encoding lipoamide dehydrogenase (LPDH), is subject to catabolite repression. The promoter of this gene contains a number of motifs for DNA-binding transcriptional activators, including three which show strong sequence homology to the core HAP2/HAP3/HAP4 binding motif. Here we report that transcription of LPD1 requires HAP2, HAP3 and HAP4 for release from glucose repression. In the wild-type strain, specific activity of LPDH was increased 12-fold by growth on lactate, 10-fold on glycerol and four- to five-fold on galactose or raffinose, compared to growth on glucose. In hap2, hap3 and hap4 null mutants, the specific activities of LPDH in cultures grown on galactose and raffinose showed only slight induction above the basal level on glucose medium. Similar results were obtained upon assaying for β-galactosidase production in wild-type, or hap2, hap3 or hap4 mutant strains carrying a single copy of the LPD1 promoter fused in frame to the lacZ gene of Escherichia coli and integrated at the URA3 locus. Transcript analysis in wild-type and hap2 mutants confirmed that the HAP2 protein regulates LPD1 expression at the level of transcription in the same way as it does for the CYC1 gene. Site-directed mutagenesis of the putative HAP2/HAP3/HAP4 binding site at −204 relative to the ATG start codon showed that this element was required for full derepression of the LPD1 gene on non-fermetable substrates.
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    URL: http://dx.doi.org/10.1007/BF00279803
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    The CDC26 gene of Saccharomyces cerevisiae is required for cell growth only at high temperature (1992)
    Springer
    Molecular genetics and genomics 231 (1992), S. 329-331 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Cell division cycle ; CDC26 ; Nuclear division
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We have cloned and sequenced the wild-type CDC26 gene and a mutant allele, cdc26-1, of Saccharomyces cerevisiae. Nucleotide sequence analysis revealed that the gene we cloned was the same as SCD26, a dosage-dependent suppressor of cdc26. However, the cloned gene is in fact the CDC26 gene, because a nucleotide substitution in cdc26-1 was found to be a nonsense mutation in this sequence. Disruption of this gene conferred thermosensitive cell growth and the disrupted cdc26 gene could not complement the cdc26-1 mutant allele. Thus, the CDC26 gene is required for cell growth only at high temperature.
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    URL: http://dx.doi.org/10.1007/BF00279807
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    Characterization of a staurosporine- and temperature-sensitive mutant, stt1, of Saccharomyces cerevisiae: STT1 is allelic to PKC1 (1992)
    Springer
    Molecular genetics and genomics 231 (1992), S. 337-344 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Staurosporine ; Protein kinase C ; Cell cycle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Staurosporine is an antibiotic that specifically inhibits protein kinase C. Fourteen staurosporine- and temperature-sensitive (stt) mutants of Saccharomyces cerevisiae were isolated and characterized. These mutants were divided into ten complementation groups, and characterized for their cross-sensitivity to K-252a, neomycin, or CaCl2, The STT1 gene was cloned and sequenced. The nucleotide sequence of the STT1 gene revealed that STT1 is the same gene as PKC1. The STT1 gene conferred resistance to staurosporine on wild-type cells, when present on a high copy number plasmid. STT1/stt1::HIS3 diploid cells were more sensitive to staurosporine than STT1/STT1 diploid cells. Analysis of temperature-sensitive stt1 mutants showed that the STT1 gene product functioned in S or G2/M phase. These results suggest that a protein kinase (the STT1 gene product) is one of the essential targets of staurosporine in yeast cells.
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    SCM4, a gene that suppresses mutant cdc4 function in budding yeast (1992)
    Springer
    Molecular genetics and genomics 235 (1992), S. 285-291 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Cell cycle ; CDC4 ; Suppression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The gene SCM4 encodes a protein which suppresses a temperature-sensitive allele of the cell division cycle gene CDC4 in Saccharomyces cerevisiae. SCM4 was cloned on a 1.8 kb BamHI fragment of yeast genomic DNA in the high copy-number vector pJDB207, which results in a 50- to 100-fold increase in the level of the 700 nucleotide SCM4 transcript in vivo. The SCM4 gene encodes a 20.2 kDa protein of 187 aminoacids with a clear tripartite domain structure in which a region rich in charged residues separates two domains of largely uncharged amino acids. Although the apparent allele specificity of cdc4 suppression suggests that the CDC4 and SCM4 proteins interact, disruption of SCM4 demonstrates that the gene product is not essential for mitosis or meiosis; however, it may be a member of a family of related, functionally redundant proteins.
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    URL: http://dx.doi.org/10.1007/BF00279372
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    Influence of DNA repair defects (radl, rad52) on nitrogen mustard mutagenesis in yeast (1992)
    Springer
    Molecular genetics and genomics 235 (1992), S. 304-310 
    Details
    ISSN: 1617-4623
    Keywords: Excision repair (RAD1) ; Mutational specificity ; Nitrogen mustard ; Saccharomyces cerevisiae ; Double-strand break repair (RAD52)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Nitrogen mustard (HN2) mutagenesis of a plasmid-borne copy of the Saccharomyces cerevisiae SUP4-o gene was examined in a repair-proficient yeast strain and isogenic derivatives defective for excision (radl) or DNA double-strand break (rad52) repair. The excision repair deficiency sensitized the cells to killing by HN2 and abolished mutation induction. Inactivation of RAD52 had no influence on the lethality of HN2 treatment but diminished the induced mutation frequency by 50% at all doses tested. DNA sequence analysis of HN2-induced SUP4-o mutations suggested that RAD52 contributed to the production of basepair substitutions at G·C sites. The rad52 defect appeared to alter the distribution of G·C → A·T transitions in SUP4-o relative to the distribution for the wild-type strain. This difference did not seem to be due to an effect of RAD52 on the relative fractions of HN2-induced transitions at localized (flanked by A·T pairs) or contiguous (flanked by at least one G·C pair) G·C sites but instead to an influence on the strand specificity of HN2 mutagenesis. In the repair-proficient strain, the transitions showed a small bias for sites having the guanine on the transcribed strand and this preference was eliminated by inactivation of RAD52.
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    URL: http://dx.doi.org/10.1007/BF00279374
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    Downstream activating sequence within the coding region of a yeast gene: specific binding in vitro of RAP1 protein (1992)
    Springer
    Molecular genetics and genomics 236 (1992), S. 65-75 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; SRP1 ; Yeast downstream activating sequence ; RAP1/GRF1 binding sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Using a gel retardation assay, a protein factor that specifically interacts with a 33 by intragenic sequence of the highly expressed and glucose-inducible SRP1 gene of Saccharomyces cerevisiae has been detected. This binding site is located in a transcribed region and within the open reading frame (positions +710 to +743 relative to the first base of the initiation codon). A mutant strain carrying a deletion of this binding site showed a dramatic decrease in steady-state levels of SRP1 transcripts. This decline is not the result of a decrease in mRNA stability, since expression of hybrid genes in which the SRP1 promoter was replaced by the heterologous CYC1 promoter was not affected by the binding site deletion. These findings suggest that the 33 by sequence contains a cis-acting downstream activating element which is involved in the transcriptional activation of the SRP1 promoter. Sequence comparisons showed similarities between a site located within the 33 by sequence and the high-affinity consensus binding site of the RAP1/GRF1 (also named TUF) factor and methylation interference experiments confirmed that this site was involved in the protein-DNA interaction. Both the results of competition experiments with upstream activating sequences of ribosomal protein genes (UASrpg), which are targets for RAP1 binding, and determination of the apparent molecular weight of the affinity-purified DNA-binding protein indicated that RAP1 factor recognized the SRP1 33 by element. The 33 by sequence was found to be unable to provide UAS activity when placed upstream of the TATA box and transcription start site.
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    URL: http://dx.doi.org/10.1007/BF00279644
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    Bending of DNA segments with Saccharomyces cerevisiae autonomously replicating sequence activity, isolated from basidiomycete mitochondrial linear plasmids (1993)
    Springer
    Molecular genetics and genomics 237 (1993), S. 1-9 
    Details
    ISSN: 1617-4623
    Keywords: DNA bending ; Autonomously replicating sequence ; Saccharomyces cerevisiae ; Basidiomycete ; Linear plasmid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Previous studies have indicated that DNA bending is a general structural feature of sequences (ARSs) from cellular DNAs of yeasts and nuclear and mitochondrial genomic DNAs of other eukaryotes that are capable of autonomous replication in Saccharomyces cerevisiae. Here we showed that bending activity is also tightly associated with S. cerevisiae ARS function of segments cloned from mitochondrial linear DNA plasmids of the basidiomycetes Pleurotus ostreatus and Lentinus edodes. Two plasmids, designated pLPO2-like (9.4 kb), and pLPO3 (6.6 kb) were isolated from a strain of P. ostreatus. A 1029 by fragment with high-level ARS activity was cloned from pLPO3 and it contained one ARS consensus sequence (A/T)TTTAT(A/G)TTT(A/T) indispensable for activity and seven dispersed ARS consensus-like (10/11 match) sequences. A discrete bent DNA region was found to lie around 500 by upstream from the ARS consensus sequence (T-rich strand). Removal of the bent DNA region impaired ARS function. DNA bending was also implicated in the ARS function associated with a 1430 by fragment containing three consecutive ARS consensus sequences which had been cloned from the L. edodes plasmid pLLE1 (11.0 kb): the three consecutive ARSs responsible for high-level ARS function occurred in, and immediately adjacent to, a bent DNA region. A clear difference exists between the two plasmid-derived ARS fragments with respect to the distance between the bent DNA region and the ARS consensus sequence(s).
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    URL: http://dx.doi.org/10.1007/BF00282777
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    Temperature sensitivity of the cdc9-1 allele of Saccharomyces cerevisiae DNA ligase is dependen on specific combinations of amino acids in the primary structure of the expressed protein (1992)
    Springer
    Molecular genetics and genomics 232 (1992), S. 332-334 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; cdc9-1 ; DNA ligase ; DNA sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In this study we present the characterization of the temperature-sensitive mutant allele cdc9-1 encoding DNA ligase, of Saccharomyces cerevisiae strain A364A by DNA sequencing. Comparison with the published wild-type sequence from strain SKI revealed 13 nucleotide exchanges between these two sequences, which are derived from non-isogenic genetic backgrounds. Only four of these changes, distributed over the whole coding region, lead to amino acid exchanges in the protein chain. Our analysis of the sequence of the wild-type CDC9 allele from strain A364A revealed differences from the isogenic cdc9-1 allele in only two nucleotides: one silent change and one leading to a single amino acid exchange. The latter is therefore responsible for the temperature-sensitive phenotype. A mosaic protein, in which a region carrying this amino acid exchange has been inserted in place of the corresponding part of CDC9 from the non-isogenic strain SKI, is not temperature sensitive. The exchange of a longer stretch of DNA leading to atteration of three amino acids of the protein compared with the original sequence of SKI is required to obtain a temperature-sensitive DNA ligase in this strain, while in strain A364A a single amino acid change is sufficient for expression of a temperature-sensitive protein.
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    URL: http://dx.doi.org/10.1007/BF00280014
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    Donation: a new, facile method of gene replacement in yeast (1993)
    Springer
    Molecular genetics and genomics 237 (1993), S. 306-310 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Gene replacement ; Donation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We describe here a new method for the introduction of non-selectable alleles into Saccharomyces cerevisiae, gene replacement by donation. This method only requires the availability of an autonomously replicating, selectable plasmid containing the allele to be introduced into yeast. The plasmid is digested at a restriction site (or sites) within this allele, and introduced into yeast by transformation. In the course of double-strand break repair, the entering plasmid donates genetic information to the chromosome, replacing the chromosomal allele in a gene conversion-like event. Gene replacement events are identified by a phenotypic screen of the transformants. When necessary, the transforming plasmid may be subsequently lost by segregation during permissive growth. We have studied several parameters affecting the utility of this protocol as a method of gene replacement. Together with our previous results, the results show gene replacement by donation to be a useful, facile method, yielding gene replacement in up to 1.5% of transformants.
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    URL: http://dx.doi.org/10.1007/BF00282812
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    Molecular structure and genetic regulation of SFA, a gene responsible for resistance to formaldehyde in Saccharomyces cerevisiae, and characterization of its protein product (1993)
    Springer
    Molecular genetics and genomics 237 (1993), S. 351-358 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Formaldehyde hyper-resistance ; Alcohol dehydrogenase ; Glutathione ; Inducibility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A 3.7 kb DNA fragment of yeast chromosome IV has been sequenced that contains the SFA gene which, when present on a multi-copy plasmid in Saccharomyces cerevisiae, confers hyper-resistance to formaldehyde. The open reading frame of SFA is 1158 by in size and encodes a polypeptide of 386 amino acids. The predicted protein shows strong homologies to several mammalian alcohol dehydrogenases and contains a sequence characteristic of binding sites for NAD. Overexpression of the SFA gene leads to enhanced consumption of formaldehyde, which is most probably the reason for the observed hyper-resistance phenotype. In sfa:LEU2 disruption mutants, sensitivity to formaldehyde is correlated with reduced degradation of the chemical. The SFA gene shares an 868 by divergent promoter with UGX2 a gene of yet unknown function. Promoter deletion studies with a SFA promoter-lacZ gene fusion construct revealed negative interference on expression of SFA by upstream sequences. The upstream region between positons − 145 and − 172 is totally or partially responsible for control of inducibility of SFA by chemicals such as formaldehyde (FA), ethanol and methyl methanesulphonate. The 41 kDa SFA-encoded protein was purified from a hyper-resistant transformant; it oxidizes long-chain alcohols and, in the presence of glutathione, is able to oxidize FA. SFA is predicted to code for a long-chain alcohol dehydrogenase (glutathione-dependent formaldehyde dehydrogenase) of the yeast S. cerevisiae.
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    URL: http://dx.doi.org/10.1007/BF00279438
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    Interchromosomal and intrachromosomal recombination in rad 18 mutants of Saccharomyces cerevisiae (1990)
    Springer
    Molecular genetics and genomics 222 (1990), S. 25-32 
    Details
    ISSN: 1617-4623
    Keywords: Intrachromosomal and interchromosomal recombination ; Saccharomyces cerevisiae ; RAD18
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The frequency of intra- and interchromosomal recombination was determined in RAD18 and rad18 deletion and rad18-3 mutant strains. It was found that spontaneous interchromosomal recombination at trp5, his1, ade2, and MAT was elevated 10- to 70-fold in the rad18-3 and rad18Δ mutants as compared to the RAD + strains. On the other hand the frequencies of spontaneous intrachromosomal recombination for the his3Δ3′, his3Δ5′ and the his4C −, his4A − duplications and for heterothallic mating type switching were only marginally elevated in the rad18 deletion mutant, and recombination between ribosomal DNA repeats was only 2-fold elevated in the rad18-3 mutant. These differences may be due to a haploid versus diploid specific difference. However interchromosomal recombination was elevated 40-fold and intrachromosomal recombination was only marginally (1.5-fold) elevated in a diploid homozygous for rad18Δ, arguing against a haploid versus diploid specific difference. Possible explanations for the difference in the elevated levels of intra- versus interchromosomal spontaneous recombination are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00283018
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    Isolation of the DLD gene of Saccharomyces cerevisiae encoding the mitochondrial enzyme D-lactate ferricytochrome c oxidoreductase (1993)
    Springer
    Molecular genetics and genomics 238 (1993), S. 315-324 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Nuclear gene ; Mitochondrial enzyme ; Lactate dehydrogenase ; Flavoprotein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract In Saccharomyces cerevisiae the utilization of lactate occurs via specific oxidation of l- and d-lactate to pyruvate catalysed by l-lactate ferricytochrome c oxidoreductase (L-LCR) (EC 1.1.2.3) encoded by the CYB2 gene, and d-lactate ferricytochrome c oxidoreductase (D-LCR) (EC 1.1.2.4), respectively. We selected several lactate− pyruvate+ mutants in a cyb2 genetic background. Two of them were devoid of D -LCR activity (dld mutants, belonging to the same complementation group). The mutation mapped in the structural gene. This was demonstrated by a gene dosage effect and by the thermosensitivity of the enzyme activity of thermosensitive revertants. The DLD gene was cloned by complementation for growth on d-, l-lactate in the strain WWF18-3D, carrying both a CYB2 disruption and the dld mutation. The minimal complete complementing sequence was localized by subcloning experiments. From the sequence analysis an open reading frame (ORF) was identified that could encode a polypeptide of 576 amino-acids, corresponding to a calculated molecular weight of 64000 Da. The deduced protein sequence showed significant homology with the previously described microsomal flavoprotein l-gulono-γ-lactone oxidase isolated from Rattus norvegicus, which catalyses the terminal step of l-ascorbic acid biosynthesis. These results are discussed together with the role of L-LCR and D-LCR in lactate metabolism of S. cerevisiae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00291989
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  • 197
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    The cauliflower mosaic virus 35S promoter is regulated by cAMP in Saccharomyces cerevisiae (1992)
    Springer
    Molecular genetics and genomics 235 (1992), S. 365-372 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; CaMV 35S promoter ; cAMP ; Transcription factors ; Heterologous expression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The cauliflower mosaic virus 35S promoter confers strong gene expression in plants, animals and fission yeast, but not in budding yeast. On investigating this paradox, we found that in budding yeast the promoter acts through two domains. Whereas the upstream domain acts as a silencer, the downstream domain couples expression to the nutritional state of the cells via the RAS/cAMP pathway. Point mutations indicate that two boxes with similarity to the cAMP regulated element (CRE) of mammalian cells mediate this response. Gel retardation assays show that, in both yeast and plant protein extracts, factors bind to this promoter element. Therefore, transcriptional activation appears to be highly conserved at the level of transcription factors and specific DNA target elements in eukaryotes. This offers new ways to investigate gene regulation mechanisms of higher eukaryotes, which are not as amenable to genetic analysis as yeast.
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    URL: http://dx.doi.org/10.1007/BF00279382
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  • 198
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    Amplification and loss of repeat units of the human minisatellite MS1 integrated in chromosome III of a haploid yeast strain (1993)
    Springer
    Molecular genetics and genomics 238 (1993), S. 38-42 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; DNA amplification ; Minisatellites ; VNTR ; MS1
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Minisatellites comprise arrays of tandemly repeated short DNA sequences which show extensive variation in repeat unit number. The mechanisms that underlie this length variation are not understood. In order to study processes influencing length changes of minisatellites, we integrated the human minisatellite MS1 into a haploid strain of the yeast Saccharomyces cerevisiae. Frequent spontaneous generation of MS1 alleles with new lengths were observed in this yeast strain. Hence it is concluded that recombination between members of a pair of homologous chromosomes is not a prerequisite for the generation of length changes in MS1 in yeast.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00279528
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  • 199
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    DNA sequence elements required for transcription initiation of the Schizosaccharomyces pombe ADH gene in Saccharomyces cerevisiae (1990)
    Springer
    Molecular genetics and genomics 223 (1990), S. 407-416 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Schizosaccharomyces pombe ; Transcription initiation ; ADH gene ; TATA sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The roles of the TATA element and sequences near the mRNA initiation site in specifying the location of initiation sites in Saccharomyces cerevisiae were examined, using the Schizosaccharomyces pombe ADH gene. The importance of spacing was demonstrated by analysis of a series of deletions that removed from 8–50 bp between the TATA element and ATG translation initiation site of this gene. Primer extension mapping showed that increasing deletion length is associated with a progressive shift downstream in the location of the initiation sites. The distance of a given site from the promoter affected the relative ability of the site to be utilized for initiation. For this gene, a permissive region for transcription initiation exists between 55 and 125 bases downstream of the TATA element, and a zone of 75–115 bases allows maximal usage of an initiation site. The presence of a TATA sequence was shown to be necessary in S. cerevisiae for maintaining the location of this “window” of initiation. The TATA sequence is essential for function of the gene in S. pombe. This gene, as well as the majority of the 63 S. cerevisiae genes surveyed, uses initiation sites which fit a PyAA/T(Pu) consensus. Cis-acting mutations were recovered which restored ADH activity to a deletion allele that initiates its mRNAs downstream of the ATG. DNA sequence and transcript analysis with these mutants confirmed the requirement of proper spacing and conformity of initiation sites to the PyAA/T(Pu) consensus for efficient transcript initiation.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00264447
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    TUF factor binds to the upstream region of the pyruvate decarboxylase structural gene (PDC1) of Saccharomyces cerevisiae (1990)
    Springer
    Molecular genetics and genomics 223 (1990), S. 449-456 
    Details
    ISSN: 1617-4623
    Keywords: Saccharomyces cerevisiae ; Gene regulation ; TUF ; Pyruvate decarboxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The upstream activation site of the pyruvate decarboxylase gene, PDC1, of Saccharomyces cerevisiae contains an RPG box, and mediates the increase in expression of a PDC1-lacZ fusion gene during growth on glucose. Oligonucleotide replacement experiments indicate that the RPG box functions as an absolute activator of expression, but other elements (possibly CTTCC repeats) are required for carbon source regulation, and maximal expression. Gel retardation and oligonucleotide competition experiments suggest that the DNA binding factor TUF interacts with the RPG box in the upstream region of PDC1. Binding of TUF factor is not carbon source dependent in in vitro experiments, and is probably not responsible for glucose induction of PDC1 expression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00264453
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