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  • Saccharomyces cerevisiae
  • Springer  (20)
  • American Meteorological Society
  • Nature Publishing Group
  • 1995-1999  (20)
  • 1990-1994
  • 1965-1969
  • 1955-1959
  • 1997  (20)
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Publisher
  • Springer  (20)
  • American Meteorological Society
  • Nature Publishing Group
  • Wiley-Blackwell  (72)
Years
  • 1995-1999  (20)
  • 1990-1994
  • 1965-1969
  • 1955-1959
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  • 1
    Electronic Resource
    Electronic Resource
    Influence of gene dosage and autoregulation of the regulatory genes INO2 and INO4 on inositol/choline-repressible gene transcription in the yeast Saccharomyces cerevisiae (1997)
    Springer
    Current genetics 31 (1997), S. 462-468 
    Details
    ISSN: 1432-0983
    Keywords: Key words Transcriptional regulation ; Phospholipid biosynthesis ; Saccharomyces cerevisiae ; INO2
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Expression of structural genes of phospholipid biosynthesis in yeast is mediated by the inositol/choline-responsive element (ICRE). ICRE-dependent gene activation, requiring the regulatory genes INO2 and INO4, is repressed in the presence of the phospholipid precursors inositol and choline. INO2 and, to a less extent, INO4 are positively autoregulated by functional ICRE sequences in the respective upstream regions. However, an INO2 allele devoid of its ICRE functionally complemented an ino2 mutation and completely restored inositol/choline regulation of Ino2p-dependent reporter genes. Low-level expression of INO2 and INO4 genes, each under control of the heterologous MET25 promoter, did not alter the regulatory pattern of target genes. Thus, upstream regions of INO2 and INO4 are not crucial for transcriptional control of ICRE-dependent genes by inositol and choline. Interestingly, over-expression of INO2, but not of INO4, counteracted repression by phospholipid precursors. Possibly, a functional antagonism between INO2 and a negative regulator is the key event responsible for repression or de-repression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050231
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  • 2
    Electronic Resource
    Electronic Resource
    A mutation in cytochrome oxidase subunit 2 restores respiration of the mutant pet ts1402 (1997)
    Springer
    Current genetics 31 (1997), S. 401-407 
    Details
    ISSN: 1432-0983
    Keywords: Key words Cytochrome oxidase ; Mitochondrial localization ; PET1402/OXA1 ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The yeast PET1402/OXA1 gene encoding a 44.8-kDa protein is required for mitochondrial biogenesis. Substitution of Leu240 to serine in the protein results in an accumulation of the precursor form of the mitochondrially encoded subunit 2 of cytochrome oxidase (Cox2) and temperature-sensitive respiration. This temperature sensitivity can be suppressed by a mutation in the cox2 gene changing Ala189 of the Cox2 protein to proline. In the cox2-ts1402 double mutant respiration is restored without removal of the Cox2 pre-sequence. The suppression suggests an interaction of the Pet1402 protein with the cytochrome oxidase complex. Antibodies raised against the predicted C-terminus and the tagged N-terminus of the Pet1402 protein reacted with a 37-kDa polypeptide. This protein, present in the mitochondrial fraction, is localized within the inner membrane. The difference in size can be explained by the removal of the predicted mitochondrial-targeting sequence from the Pet1402 protein. The mitochondrial localization of the protein points to a direct interaction with the cytochrome oxidase complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050222
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  • 3
    Electronic Resource
    Electronic Resource
    Bleomycin hydrolase (Blh1p), a multi-sited thiol protease in search of a distinct physiological role (1997)
    Springer
    Current genetics 32 (1997), S. 41-51 
    Details
    ISSN: 1432-0983
    Keywords: Key words Bleomycin hydrolase ; Saccharomyces cerevisiae ; Thiol proteases ; Protein amphitropism ; Processing of glycosyl-phosphatidylinositol (GPI) anchor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Bleomycin hydrolase, Blh1p, from yeast was co-purified with Gce1p, a cAMP-binding ectoprotein, anchored to the plasma membrane by a glycosyl-phosphatidylinositol (GPI) anchor. Blh1p is a hydrophilic thiol protease lacking transmembrane domains. We have used polyclonal antibodies to study the topology of the over-expressed protein in yeast and have found that it is amphitropic. Part of Blh1p is associated with plasma membranes, and most of the rest occurs in the cytosol. Both the growth conditions and calcium were found to have minor influences on the topology of Blh1p, in that glucose and the earth-alkali ion slightly enhanced recruitment to the membrane. We have examined the possibility that co-purification of Blh1p with Gce1p has a functional basis, and have observed that over-expression of BLH1 in yeast leads to an acceleration of the glucose-induced amphiphilic to hydrophilic conversion of Gce1p, wherein Blh1p could either directly catalyse the proteolytic removal of the polar headgroup of the GPI anchor subsequent to an initial lipolytic cleavage by a GPI-specific phospholipase C or indirectly modulate the reaction. The data show that a thiol protease is involved, but point to an indirect role of Blh1p in GPI processing. Proteases with similar or overlapping substrate specificity are likely to exist, since deletion of BLH1 neither entails a growth defect on any carbon source tested, nor the loss of proteolytic processing of the GPI anchor of Gce1p. Reduced proteolytic GPI processing is, however, observed in the blh1 mutant and the corresponding acceleration in the respective BLH1 multi-copy transformant.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050246
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  • 4
    Electronic Resource
    Electronic Resource
    Arabidopsis thaliana RAD6 homolog AtUBC2 complements UV sensitivity, but not N-end rule degradation deficiency, of Saccharomyces cerevisiae rad6 mutants (1997)
    Springer
    Current genetics 32 (1997), S. 309-314 
    Details
    ISSN: 1432-0983
    Keywords: Key words RAD6 ; Ubiquitin-conjugating enzymes ; Saccharomyces cerevisiae ; Arabidopsis thaliana
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract AtUBC2 of Arabidopsis thaliana encodes a structural homolog of the RAD6 gene of Saccharomyces cerevisiae with approximately 65% identical amino acids. Like structural homologs from other organisms, AtUBC2 lacks the carboxyl-terminal extension of mostly acidic amino acids which is present in Rad6p. AtUBC2 was expressed in S. cerevisiae rad6 mutants. It was found to partially complement the UV sensitivity and reduced growth rate of rad6 mutants at elevated temperatures. AtUBC2 however, has no apparent influence on the degradation of N-end rule substrates in the heterologous host.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002940050282
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  • 5
    Electronic Resource
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    The dual role of mRNA half-lives in the expression of the yeast ALG7 gene (1997)
    Springer
    Molecular and cellular biochemistry 169 (1997), S. 95-106 
    Details
    ISSN: 1573-4919
    Keywords: Saccharomyces cerevisiae ; N-glycosylation ; dolichol pathway ; ALG7 ; post-transcriptional regulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The yeast ALG7 gene functions by initiating the synthesis of the dolichol-linked oligosaccharide precursor and plays an important role in the control of protein N-glycosylation. The levels of ALG7 multiple transcripts are modulated by the physiological status of the cell and environmental cues, and deregulation of their abundance is deleterious to several cellular functions. Since ALG7 mRNAs are unstable, we investigated the role of these transcripts' half-lives in determining their steady-state levels. Using a temperature-sensitive RNA polymerase II mutant, we demonstrate that increased stability was the primary determinant of higher ALG7 mRNA abundance in response to glucose limitation or treatment with tunicamycin. In contrast, at the G1/G0 transition point, changes in the decay rates were inversely related to ALG7 transcript accumulation: the decreased abundance of ALG7 mRNAs following exit from the mitotic cycle was associated with lengthening of the decay rates, while their increased accumulation after growth stimulation correlated with decreased stability. This suggests that, depending on the circumstance, mRNA half-lives can either directly determine the level of ALG7 transcript accumulation or oppose regulatory changes at other control levels.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006803004151
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  • 6
    Electronic Resource
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    Site-Directed Mutagenesis in Basic Amino Acid Residues of Saccharomyces cerevisiae Phosphoenolpyruvate Carboxykinase (1997)
    Springer
    The protein journal 16 (1997), S. 233-236 
    Details
    ISSN: 1573-4943
    Keywords: Saccharomyces cerevisiae ; phosphoenolpyruvate carboxykinase ; pyridoxal phosphate ; site-directed mutagenesis
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Mutant Arg76Gln and Lys290Gln Saccharomyces cerevisiae phosphoenolpyruvate carboxykinases have been prepared and analyzed. No alteration in the apparent kinetic constants were detected for the Arg76Gln mutant enzyme, while the Lys290Gln mutant showed a 12-fold decrease in V max/K mADP. These results indicate that Arg76 is not involved in CO2 binding, but support the hypothesis that the binding of this substrate induces a conformational change that protects the region around Arg76 from trypsin action [Herrera et al. (1993) J. Protein Chem. 12, 413–418]. These findings also indicate that Lys290, a highly reactive residue against pyrydoxal phosphate [Bazaes et al. (1995), FEBS Lett. 360, 207–210], does not perform an essential function for the enzyme activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1026335010370
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  • 7
    Electronic Resource
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    Yeast Crv4/Ttp1, a predicted type II membrane protein, is involved in an event important for growth, functionally overlapping with the event regulated by calcineurin- and Mpk1-mediated pathways (1997)
    Springer
    Molecular genetics and genomics 256 (1997), S. 481-487 
    Details
    ISSN: 1617-4623
    Keywords: Key words Calcineurin ; Mpk1 MAP kinase ; Type II membrane protein ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The Saccharomyces cerevisiae crv mutants (crv1, 2, 3 and 4) exhibit phenotypes, such as calcium resistance and vanadate sensitivity, which are apparently similar to those of calcineurin-deficient mutants. We have cloned and characterized the CRV4 gene that complements all the phenotypes of the crv4 mutant. DNA sequencing revealed that CRV4 is identical to the previously cloned gene TTP1, which encodes a type II membrane protein of unknown function. Deletion of CRV4/TTP1 causes no obvious phenotype except for Ca2+ resistance and vanadate sensitivity, but is synthetically lethal in combination with a deletion of MPK1, in a manner which is suppressible by the addition of an osmotic stabilizer. In medium containing sorbitol as an osmotic stabilizer, the cnb1 mpk1 ttp1 triple mutant exhibits a more severe growth defect than does any of the double mutants cnb1 ttp1, cnb1 mpk1 or mpk1 ttp1. A high Ca2+ concentration (50 mM) or a constitutively active form of calcineurin partially suppresses the growth defect of the mpk1 ttp1 double mutant. These results indicate that Ttp1 participates in a cellular event essential for growth and morphogenesis, in parallel with the pathways involving Mpk1 MAP kinase and calcineurin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050592
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  • 8
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    The STT3 protein is a component of the yeast oligosaccharyltransferase complex (1997)
    Springer
    Molecular genetics and genomics 256 (1997), S. 628-637 
    Details
    ISSN: 1617-4623
    Keywords: Key words N-linked glycosylation ; Endoplasmic reticulum ; Oligosaccharyltransferase ; STT3 ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract N-linked protein glycosylation is an essential process in eukaryotic cells. In the central reaction, the oligosaccharyltransferase (OTase) catalyzes the transfer of the oligosaccharide Glc3Man9GlcNAc2 from dolicholpyrophosphate onto asparagine residues of nascent polypeptide chains in the lumen of the endoplasmic reticulum. The product of the essential gene STT3 is required for OTase activity in vivo, but is not present in highly purified OTase preparations. Using affinity purification of a tagged Stt3 protein, we now demonstrate that other components of the OTase complex, namely Ost1p, Wbp1p and Swp1p, specifically co-purify with the Stt3 protein. In addition, different conditional stt3 alleles can be suppressed by overexpression of either OST3 and OST4, which encode small components of the OTase complex. These genetic and biochemical data show that the highly conserved Stt3p is a component of the oligosaccharyltransferase complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050611
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  • 9
    Electronic Resource
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    Isolation of giant mitochondrial nucleoids from the yeastSaccharomyces cerevisiae (1997)
    Springer
    Protoplasma 198 (1997), S. 177-185 
    Details
    ISSN: 1615-6102
    Keywords: Yeast ; Saccharomyces cerevisiae ; Mitochondrial nucleoids ; DNA-binding proteins ; Anaerobic culture
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The yeast cellsSaccharomyces cerevisiae grown up to stationary phase under either anaerobic conditions, or aerobic conditions in the presence of a respiratory inhibitor, antimycin A, had distinctive giant mitochondrial nucleoids (mt-nucleoids) (apparent diameter 0.6–0.9 μm) in contrast with the small mt-nucleoids (apparent diameter 0.2–0.4 μm) in respiratory-sufficient cells grown aerobically, as revealed by DAPI-fluorescence microscopy. The cytoplasmic respiratory-deficient cells (rho− cells), which were induced by treatment of wild-type cells with ethidium bromide, showed both giant and small mt-nucleoids of irregular size. In order to examine the structural and functional differences between giant and small mt-nucleoids, the former were successfully isolated from spheroplasts of three different cells by differential centrifugation and centrifugation on a discontinuous sucrose gradient. The isolated giant mt-nucleoids were intact in the morphology and were free of significant contamination by nuclear chromatin. The number of protein components involved in each of three different giant mt-nucleoids was similar to the number in small mt-nucleoids from aerobically grown cells, though a few noticeable differences were also recognized. DNA-binding proteins with molecular masses of 67 kDa, 52 kDa, 50 kDa, 38 kDa, 26 kDa, and 20 kDa were the main components of small mt-nucleoids from aerobically grown cells as detected by chromatography on native DNA-cellulose. In contrast, the 67 kDa and 52 kDa proteins were hardly detected in corresponding fractions of giant mt-nucleoids from anaerobically grown cells and from rho− cells grown aerobically. On the other hand, mt-nucleoids from aerobically grown cells in the presence of antimycin A seemed to lack the 67 kDa protein but to have a small amount of the 52 kDa protein. This is the first demonstration of the variance of protein species involved in yeast mt-nucleoids according to the respiratory activity of mitochondria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01287567
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  • 10
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    Rig2, a RING finger protein that interacts with the Kin28/Ccl1 CTD kinase in yeast (1997)
    Springer
    Molecular genetics and genomics 255 (1997), S. 460-466 
    Details
    ISSN: 1617-4623
    Keywords: Key words Transcription ; TFIIH ; MAT1 ; RING finger protein ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Kin28/Ccl1, a cyclin-dependent kinase, is essential for the in vivo phosphorylation of the C-terminal domain of the largest subunit of RNA polymerase II in Saccharomyces cerevisiae. In a search for mutations co-lethal with a thermosensitive kin28 mutation, we have identified genes whose products interact functionally with Kin28. In the present work, we have studied a new complementation group of synthetic lethal mutations. The corresponding gene, RIG2, encodes a predicted RING finger protein. Rig2 is likely to be a homolog of MAT1 of higher eukaryotes which forms a ternary complex with MO15(cdk7) and cyclin H. Our genetic data suggest that Rig2 is a component of transcription factor TFIIH. Transcription activity in a rig2-ts mutant is impeded at restrictive temperature. However, none of the rig2-ts mutants obtained was UV sensitive, suggesting that Rig2 is dispensable for nucleotide excision repair.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050518
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  • 11
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    Overexpression of the protein kinase Pak1 suppresses yeast DNA polymerase mutations (1997)
    Springer
    Molecular genetics and genomics 256 (1997), S. 45-53 
    Details
    ISSN: 1617-4623
    Keywords: Key words Protein phosphorylation ; DNA replication ; Cell cycle checkpoint ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract This article presents the identification and characterization of the PAK1 gene of Saccharomyces cerevisiae, and the biochemical characterization of the protein kinase activity that it encodes. Overexpression of the PAK1 gene product suppresses temperature-sensitive mutations of the pol1 (cdc17) gene, which encodes DNA polymerase α. Overexpression and suppression can be achieved either by expressing PAK1 from a high-copy-number plasmid, or by GAL1-induced transcription of PAK1. Gene disruption of PAK1 indicates that it is not an essential gene. The PAK1 gene encodes a protein with a kinase consensus domain. By deletion analysis and site-directed mutagenesis, we demonstrate that the complete and active kinase consensus domain is required for suppression. A glutathione-S-transferase (GST)-Pak1 fusion protein, overproduced in bacteria, can be purified in an active form with glutathione affinity beads or by immunoprecipitation. Thus, other protein subunits of Pak1 are not required for its activity. In vitro protein kinase assays show that GST-Pak1 can autophosphorylate, and can phosphorylate casein as an exogenous substrate. The phenotype of the suppressed cdc17-1 cells indicates that Pak1 suppression is inefficient and does not restore the wild-type phenotype. Pak1 suppression requires Rad9 function, but Pak1 does not affect Rad9 function. Overexpression of PAK1 does not enhance the expression of the POL1 gene. Pak1 may function by modifying and partially stabilizing thermolabile DNA polymerases, perhaps during DNA repair, because pak1 mutant cells are caffeine sensitive.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050544
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  • 12
    Electronic Resource
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    A defect in GTP synthesis affects mannose outer chain elongation in Saccharomyces cerevisiae (1997)
    Springer
    Molecular genetics and genomics 256 (1997), S. 469-480 
    Details
    ISSN: 1617-4623
    Keywords: Key words GMP kinase ; GDP-mannose synthesis ; N-glycosylation ; Mannose outer chain elongation ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We have found that yeast mutants that are defective in mannose outer chain elongation of N-linked glycoproteins show higher cell wall porosity than normal cells, and are hypersensitive to antibiotics with a large molecular weight; such as neomycin and geneticin. Wild-type yeast cells also showed enhanced sensitivity to neomycin in the presence of tunicamycin, an inhibitor of N-glycosylation, suggesting that the extent of N-glycosylation may affect the sensitivity of yeast cells to drugs and that sensitivity to neomycin may be an effective method for screening for yeast mutants defective in N-glycosylation. Pursuing this logic, we isolated neomycin-sensitive yeast mutants and screened them for defects in N-glycosylation. The neomycin-sensitive, N-glycosylation-defective mutants fell into 15 complementation groups including alleles of the previously isolated temperature-sensitive nes mutants nes10, nes17, and nes25. Gene cloning revealed that NES10 was identical to SEC20, which is involved in ER-Golgi protein transport. NES17 was identical to ALG1, which encodes a β-1,4-mannosyltransferase present in the ER. MSN17, a multicopy suppressor of nes17/alg1, was also isolated and found to be an allele of PSA1, which is involved in GDP-mannose synthesis. NES25 was identical to GUK1, which encodes a GMP kinase. Overexpression of MSN17 increased the GDP-mannose level in a wild-type strain by about threefold, and guk1 decreased the GDP-mannose level to one-fourth, suggesting a close relationship between GTP metabolism and mannose outer chain elongation; the link is presumably provided by the process of GDP-mannose transport in the Golgi membranes.
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    URL: http://dx.doi.org/10.1007/s004380050591
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  • 13
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    The general regulatory factor Reb1p controls basal, but not Gal4p-mediated, transcription of the GCY1 gene in yeast (1997)
    Springer
    Molecular genetics and genomics 256 (1997), S. 682-689 
    Details
    ISSN: 1617-4623
    Keywords: Key words General regulatory factors ; Gal4 protein ; Saccharomyces cerevisiae ; Basal transcription
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Expression of the gene GCY1 in Saccharomycescerevisiae is induced by about 25-fold in the presence of galactose as a result of activation by Gal4p. In contrast to other Gal4p-regulated genes, such as GAL1 or GAL10, GCY1 is transcribed at a relatively high basal level. We have analysed the basis of this behaviour and have found that, in addition to a UAS GAL , a binding site for the general regulatory factor Reb1p is localized 100 bp upstream of the TATA sequence and about 140 bp 3′ to the UAS GAL . Reb1p binds to this site with low affinity. Reb1p, an abundant, multifunctional DNA-binding protein in yeast, acts as a weak transcriptional activator in the control regions of several genes encoding unrelated functions. The action of Reb1p is assumed to be strongly position dependent. In the control region of GCY1, Reb1p acts independently of position and stimulates basal expression of GCY1 about threefold, whereas Gal4p-mediated activation is not influenced significantly. Promoter-proximal insertion of an additional Reb1p recognition site enhances basal transcription only marginally, but can largely compensate for deletion of the natural Reb1p-binding site. Either an Abf1p- or a Rap1p-binding site can substitute for the Reb1p recognition sequence, indicating that these general regulatory factors fulfill related functions in basal transcription, without affecting Gal4p-mediated activation. In addition to Reb1p, the sequence of the Gal4p-binding site influences basal transcription. This effect is independent of the Gal4 protein, as it operates in a gal4 mutant background as well. This finding suggests that the nucleotide sequence of the UAS GAL in the GCY1 promoter has intrinsic properties, presumably a particular DNA structure, that influence basal transcription and act synergistically with Reb1p.
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    URL: http://dx.doi.org/10.1007/s004380050616
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  • 14
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    Characterization of an AP-1-like transcription factor that mediates an oxidative stress response in Kluyveromyces lactis (1997)
    Springer
    Molecular genetics and genomics 257 (1997), S. 62-70 
    Details
    ISSN: 1617-4623
    Keywords: Key words YAP1 ; Kluyveromyces lactis ; Saccharomyces cerevisiae ; Transcriptional activator ; Oxidative stress response
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The KlYAP1 gene, encoding the transcription factor Yap1p from Kluyveromyces lactis, was cloned by functional complementation of the cadmium hypersensitivity phenotype of a Saccharomyces cerevisiae strain lacking functional YAP1 and YAP2 genes. The KlYAP1 gene product is 41% identical to Yap1p, the sequence similarity being centered on the bZip domain and extending into the C-terminal portion of both proteins. When expressed in S. cerevisiae, this gene efficiently complements some of the phenotypes associated with both yap1 and yap2 mutations and also mediates AP-1 response element-dependent transcriptional activation in response to H2O2. Gene disruption experiments in K. lactis indicated that the KlYAP1 gene is involved in both the oxidative and cadmium response pathways. We also demonstrate the existence in K. lactis of inducible protective stress responses to both peroxides and superoxides and investigate the role of the Klyap1p protein in these responses.
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    URL: http://dx.doi.org/10.1007/s004380050624
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  • 15
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    Vacuolar acidification in Saccharomyces cerevisiae induced by elevated hydrostatic pressure is transient and is mediated by vacuolar H+-ATPase (1997)
    Springer
    Extremophiles 1 (1997), S. 89-93 
    Details
    ISSN: 1433-4909
    Keywords: Key words Hydrostatic pressure ; Saccharomyces cerevisiae ; Transient vacuolar acidification ; Vacuolar H+-ATPase ; Chemical reaction of CO2
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract We analyzed the vacuolar acidification in response to elevated hydrostatic pressure in Saccharomyces cerevisiae. The vacuolar pH, defined using 6-carboxyfluorescein, was directly measured in a hyperbaric chamber with a transparent window under high hydrostatic pressure. The vacuole of strain X2180 became acidified at the onset of pressurization to an extent dependent on the magnitude of pressure applied. A pressure of 40–60 MPa transiently reduced the vacuolar pH by about 0.33 within 4 min. The transient acidification was observed in the presence of D-glucose, D-fructose, or D-mannose as a carbon source, but not 3-o-methyl-D-glucose, ethanol, or glycerol, suggesting that the generation of CO2 was involved in the process. A vma3 mutant defective in vacuolar acidification showed no reduction of vacuolar pH when hydrostatic pressure was applied. This result indicates that the transient vacuolar acidification induced by elevated hydrostatic pressure is mediated through the function of the vacuolar H+-ATPase.
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    URL: http://dx.doi.org/10.1007/s007920050019
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  • 16
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    Molecular genetic and biochemical analysis of Brassica napus proliferating cell nuclear antigen function (1997)
    Springer
    Plant molecular biology 34 (1997), S. 693-700 
    Details
    ISSN: 1573-5028
    Keywords: Brassica napus ; complementation ; DNA polymerase δ ; DNA replication ; proliferating cell nuclear antigen (PCNA) ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A cDNA encoding the proliferating cell nuclear antigen (PCNA) from Brassica napus (oilseed rape) was shown to complement the lethal deletion mutation in the PCNA gene (ΔPOL30) of Saccharomyces cerevisiae. We provide unequivocal evidence that the B. napus PCNA can perform all the essential functions of the yeast PCNA in DNA replication, although some species-specific differences may exist. In addition, the B. napus PCNA expressed as a fusion polypeptide with glutathione S-transferase (GST) was shown to stimulate the activity and processivity of two δ-like DNA polymerases from wheat in vitro. These experiments provide direct biochemical evidence that the B. napus PCNA may function as an auxiliary factor in plant cell DNA replication.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005817220344
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  • 17
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    The use of monochloroacetic acid for improved ethanol production by immobilized Saccharomyces cerevisiae (1997)
    Springer
    World journal of microbiology and biotechnology 14 (1997), S. 107-111 
    Details
    ISSN: 1573-0972
    Keywords: Glutaraldehyde ; immobilization ; monochloroacetic acid ; Saccharomyces cerevisiae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008888820176
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  • 18
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    Modulation of sporulation and metabolic fluxes in Saccharomyces cerevisiae by 2 deoxy glucose (1997)
    Springer
    Antonie van Leeuwenhoek 72 (1997), S. 283-290 
    Details
    ISSN: 1572-9699
    Keywords: Sporulation ; Saccharomyces cerevisiae ; 2 deoxy glucose ; metabolic fluxes ; gluconeogenesis ; glyoxylate cycle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Quantitative studies of metabolic fluxes during Saccharomyces cerevisiae sporulation on acetate in the presence of the glucose analog, 2-deoxy glucose (2dG) are reported. We have studied the inhibition of sporulation and associated catabolic or anabolic fluxes by 2dG. Sporulation frequencies decreased from 50% to 2% asci per cell at 2dG concentrations in the range of 0.03 to 0.30 g l〉-1, respectively. Under the same conditions, the acetate consumption flux was inhibited up to 60% and the glyoxylate cycle and gluconeogenic fluxes decreased from 0.7 and 0.3 mmol h〉-1 g〉-1 dw, respectively, to negligible values. We observed a linear correlation of the acetate consumption rate with the sporulation frequency by varying the 2dG concentration. The linear correlation was also verified between the frequency of sporulation and the fluxes through glyoxylate cycle and gluconeogenic pathways. In addition, the same association of inhibition of sporulation and metabolic fluxes was found in other S. cerevisiae strains displaying different potentials of sporulation. The results presented suggest that inhibition of sporulation in the presence of the glucose analog may be attributed, at least in part, to the inhibition of anabolic fluxes and might be associated with catabolite repression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1000465110758
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  • 19
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    Electronic Resource
    Isolation and characterization of mutants resistant to amino acid analogues obtained from Saccharomyces cerevisiae strains (1997)
    Springer
    World journal of microbiology and biotechnology 14 (1997), S. 243-246 
    Details
    ISSN: 1573-0972
    Keywords: Amino acid analogue ; Saccharomyces cerevisiae ; secondary products ; wine yeast ; winemaking
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Mutants resistant to the amino acid analogues dl-thiaisoleucine, dl-4-azaleucine, 5,5,5-trifluoro-dl-leucine and l-O-methylthreonine, were isolated from Saccharomyces cerevisiae wine yeast strains. The fermentative production of secondary metabolites by the mutants was tested in grape must. Higher alcohols, acetaldehyde and acetic acid concentration varied depending on strain and analogue. Most of the mutants produced increased amounts of amyl alcohol. A remarkable variability in the level of n-propanol, isobutanol, acetaldehyde and acetic acid was observed. In practical application, the use of mutants resistant to amino acid analogues can improve the quality of wines by reducing or increasing the presence of some secondary compounds.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1008842431988
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  • 20
    Electronic Resource
    Electronic Resource
    Differences between pectic enzymes produced by laboratory and wild-type strains of Saccharomyces cerevisiae (1997)
    Springer
    World journal of microbiology and biotechnology 13 (1997), S. 711-712 
    Details
    ISSN: 1573-0972
    Keywords: Endopolygalacturonase ; pectic enzymes ; Saccharomyces cerevisiae ; yeast
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The laboratory strain of S. cerevisiae, IM1-8b, showed pectolytic activity in the presence of either glucose, fructose, or sucrose as the carbon source, but not with galactose. The enzyme activity was rapidly lost with shaking. The optimum pH and temperature for activity were 4.5 and 45°C, respectively. The enzyme was an endopolygalacturonase, since it preferentially hydrolysed pectate over pectin and decreased the viscosity of a 5% polygalacturonic solution by about 30% in 30min producing oligogalacturonic acid and digalacturonic acid as end-products.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1018587425202
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