Search results for "FUNGAL"

showing 10 items of 1116 documents

Modulation of the glycerol and ethanol syntheses in the yeast Saccharomyces kudriavzevii differs from that exhibited by Saccharomyces cerevisiae and …

2010

In the last years there is an increasing demand to produce wines with higher glycerol levels and lower ethanol contents. The production of these compounds by yeasts is influenced by many environmental variables, and could be controlled by the choice of optimized cultivation conditions. The present work studies, in a wine model system, the effects of temperature, pH and sugar concentration on the glycerol and ethanol syntheses by yeasts Saccharomyces cerevisiae T73, the type strain of Saccharomyces kudriavzevii IFO 1802(T), and an interspecific hybrid between both species (W27), which was accomplished by the application of response surface methodology based in a central composite circumscrib…

GlycerolWineFungal proteinEthanolEthanolbiologySaccharomyces cerevisiaeGlycerolphosphate DehydrogenaseSaccharomyces cerevisiaebiology.organism_classificationMicrobiologySaccharomycesYeastFungal ProteinsSaccharomyceschemistry.chemical_compoundBiochemistrychemistryGlycerolSaccharomyces kudriavzeviiFood ScienceFood Microbiology
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Differential expression of the invertase-encoding SUC genes in Saccharomyces cerevisiae

1992

Invertase (INV) is encoded in Saccharomyces cerevisiae by a family of genes, comprising SUC1-SUC5 and SUC7. Production of INV is highly variable, dependent on the strain and SUC gene present in the cell. The differences in INV production derive from the structure of the genes or are dependent on the genetic background of the strain. Centromeric plasmids (based on YCp50) carrying one of the SUC genes (except SUC7) were introduced into a strain (SEY2101) lacking SUC genes. The INV produced by the transformants was dependent on the individual SUC genes, and correlated with INV mRNA levels. Plasmids in which SUC2 had been placed under control of promoters from the other SUC genes, were used to …

Glycoside HydrolasesGenes FungalMolecular Sequence DataSaccharomyces cerevisiaeSaccharomyces cerevisiaeRegulatory Sequences Nucleic AcidGene Expression Regulation EnzymologicPlasmidTranscription (biology)Gene Expression Regulation FungalGene expressionGeneticsRNA MessengerPromoter Regions GeneticGeneGeneticsBase Sequencebeta-FructofuranosidasebiologyNucleic acid sequenceRNA FungalPromoterGeneral Medicinebiochemical phenomena metabolism and nutritionbiology.organism_classificationMolecular biologyRegulatory sequenceGene
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Phenotype traits associated with different alleles at the RPS5 locus in Saccharomyces cerevisiae

1992

The RPS5 gene has been characterised through its ability to reduce invertase production by the SUC5 gene. In this paper we show that RPS5 acts by maintaining low levels of SUC5 mRNA. We also show that RPS5 acts on the SUC1 and SUC4 genes but not on SUC2 and SUC3, which are members of the SUC family. RPS5 also shows a pleiotropic effect on the amount of mitochondrial cytochromes.

Glycoside HydrolasesTranscription GeneticGenes FungalSaccharomyces cerevisiaeGenes RecessiveLocus (genetics)Saccharomyces cerevisiaeSaccharomycesGene Expression Regulation EnzymologicGene Expression Regulation FungalGenes RegulatorGene expressionGeneticsAlleleGeneAllelesGenes DominantRegulator geneGeneticsbeta-FructofuranosidasebiologyGeneral Medicinebiology.organism_classificationPhenotypePhenotypeCytochromesCurrent Genetics
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Molecular events associated with glucose repression of invertase in Saccharomyces cerevisiae.

1986

When S. cerevisiae growing in the presence of glucose (repressive condition) was shifted to higher temperatures, invertase was secreted. This secretion required protein synthesis, but was independent of RNA formation (Mormeneo & Sentandreu 1982). In addition accumulation of invertasespecific messenger RNA occurred in the absence of protein synthesis but was expressed only after synthesis of protein. Invertase mRNA was continuously synthesized under repressive conditions and the levels of this mRNA were regulated by the presence of glucose. The hexose regulated the concentration of this mRNA at the level of transcription and/or by sensitization of this messenger RNA. The expression of the in…

Glycoside HydrolasesTranscription GeneticSaccharomyces cerevisiaeSaccharomyces cerevisiaeCycloheximideBiologyMicrobiologyEnzyme Repressionchemistry.chemical_compoundTranscription (biology)Protein biosynthesisRNA MessengerCycloheximideMaltoseMolecular BiologyMessenger RNAbeta-FructofuranosidaseTemperatureRNA FungalGeneral MedicineMaltosebiology.organism_classificationCulture MediaInvertaseGlucoseBiochemistrychemistryEnzyme RepressionAntonie van Leeuwenhoek
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DNase I sensitivity of the chromatin of the yeast SUC2 gene for invertase.

1986

The DNase I sensitivity of chromatin of the yeast SUC2 gene, which encodes two forms of invertase, has been studied both in the genome and in a multicopy plasmid carrying the gene and its flaking sequences. Whereas little if any difference in the DNase I sensitivity of the flanking regions was found between the repressed and the derepressed states, derepression of the gene was accompanied by a large increase in the sensitivity of the transcribed region. A well-defined DNase I hypersensitive site was found centered at approximately 120 bp downstream from the end of the coding region. This site seems to be flanked in the 3' non-coding region by strictly positioned nucleosomes, and the structu…

Glycoside Hydrolasesbeta-FructofuranosidaseTATA boxGenes FungalSaccharomyces cerevisiaeBiologyMolecular biologyChromatinGenesRegulatory sequenceGeneticsCoding regionNucleosomeDeoxyribonuclease IDNase I hypersensitive siteDeoxyribonuclease IMolecular BiologyHypersensitive siteDerepressionPlasmidsMoleculargeneral genetics : MGG
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Evidence for the formation of covalent bonds between macromolecules in the domain of the wall of Candida albicans mycelial cells

1989

An O-glycosylated mannoprotein, after its incorporation into the wall, showed an increase in its molecular weight, due at least to its association with N-glycosidic sugar chain(s). This was shown by rendering the material soluble after partial degradation of the wall structure. At present it is unknown whether this phenomenon is due to an additional transglycosylation process or whether the partial degradation of the wall solubilizes a supramolecular structure formed between the original O-glycosylated protein which becomes linked either directly or indirectly through a protein to the N-sugar chain(s).

GlycosylationMacromolecular SubstancesBlotting WesternBiophysicsSupramolecular chemistryPolysaccharideBiochemistryFungal ProteinsCell wallCell WallCandida albicansCandida albicansMolecular Biologychemistry.chemical_classificationGel electrophoresisMembrane Glycoproteinsbiologybeta-GlucosidaseAntibodies MonoclonalGlucan 13-beta-GlucosidaseCell Biologybiology.organism_classificationMolecular Weightcarbohydrates (lipids)ProteoglycanBiochemistrychemistryCovalent bondbiology.proteinBiophysicsProtein Processing Post-TranslationalMacromoleculeBiochemical and Biophysical Research Communications
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Identification of Two Mannoproteins Released from Cell Walls of a Saccharomyces cerevisiae mnn1 mnn9 Double Mutant by Reducing Agents

1999

The cell wall of Saccharomyces cerevisiae represents some 30% of the total weight of the cell and is made up of β-glucans, mannose-containing glycoproteins (mannoproteins), and small amounts of chitin (9, 15). The mannoproteins can be divided into three groups according to the linkages that bind them to the structure of the cell wall: (i) noncovalently bound, (ii) covalently bound to the structural glucan, and (iii) disulfide bound to other proteins that are themselves covalently bound to the structural glucan of the cell wall (8). Our work has focused on the disulfide-bound mannoproteins, probably the least well known of the three groups mentioned above. Previous work (25) showed that trea…

GlycosylationSaccharomyces cerevisiae ProteinsGlycosylationBlotting WesternMolecular Sequence DataSaccharomyces cerevisiaeSaccharomyces cerevisiaeMicrobiologyGene Expression Regulation EnzymologicFungal ProteinsCell wallOpen Reading FramesSurface-Active Agentschemistry.chemical_compoundCell WallGene Expression Regulation FungalEndopeptidasesAspartic Acid EndopeptidasesAmino Acid SequenceSubtilisinsFluorescent Antibody Technique IndirectMolecular BiologyMercaptoethanolGlucanGel electrophoresischemistry.chemical_classificationFungal proteinMembrane GlycoproteinsbiologySodium Dodecyl SulfateBiological Transportbiology.organism_classificationRecombinant ProteinsYeastMolecular Weightcarbohydrates (lipids)Cytoskeletal ProteinsEukaryotic CellsPhenotypechemistryBiochemistryMutagenesisReducing AgentsElectrophoresis Polyacrylamide GelProprotein ConvertasesProtein Tyrosine PhosphatasesGlycoproteinGene DeletionJournal of Bacteriology
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Immunochemical analysis of the carbohydrate moiety of yeast killer toxin K28

1990

Killer toxin K28, a 16 kd protein secreted by the wine yeast Saccharomyces cerevisiae strain 28, was reversibly bound by a column of Concanavalin A-Sepharose, confirming its glycoprotein nature. HPLC analysis of acid hydrolyzates of K28 toxin as well as Western-blots of beta-eliminated and/or endo H-treated killer toxin preparations probed with polyclonal alpha-toxin antibodies revealed that the carbohydrate moiety of K28 consists of D-mannose only, which is O-glycosidically linked via Ser/Thr residues to the protein part. The change in gel mobility of K28 after beta-elimination was caused by a decrease in molecular mass of about 1,800, corresponding to a carbohydrate moiety of 10 mannose r…

GlycosylationSaccharomyces cerevisiae ProteinsGlycosylationBlotting WesternSaccharomyces cerevisiaeMannoseSaccharomyces cerevisiaemedicine.disease_causeMicrobiologyChromatography Affinitychemistry.chemical_compoundmedicineMolecular BiologyAntibodies FungalChromatography High Pressure Liquidchemistry.chemical_classificationbiologyMolecular massToxinImmunochemistrySepharoseGeneral MedicineMycotoxinsbiology.organism_classificationKiller Factors YeastYeastchemistryBiochemistryPolyclonal antibodiesbiology.proteinGlycoproteinMannoseAntonie van Leeuwenhoek
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Killer toxin of Hanseniaspora uvarum

1990

The yeast Hanseniaspora uvarum liberates a killer toxin lethal to sensitive strains of the species Saccharomyces cerevisiae. Secretion of this killer toxin was inhibited by tunicamycin, an inhibitor of N-glycosylation, although the mature killer protein did not show any detectable carbohydrate structures. Culture supernatants of the killer strain were concentrated by ultrafiltration and the extracellular killer toxin was precipitated with ethanol and purified by ion exchange chromatography. SDS-PAGE of the electrophoretically homogenous killer protein indicated an apparent molecular mass of 18,000. Additional investigations of the primary toxin binding sites within the cell wall of sensitiv…

GlycosylationSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaechemical and pharmacologic phenomenaSaccharomyces cerevisiaemedicine.disease_causeHanseniasporaBiochemistryMicrobiologyMicrobiologyFungal Proteinschemistry.chemical_compoundCell WallGeneticsmedicineExtracellularSecretionIsoelectric PointGlucansMolecular BiologyBinding SitesbiologyMolecular massToxinGeneral MedicineTunicamycinMycotoxinsChromatography Ion Exchangebiology.organism_classificationKiller Factors YeastYeastBiochemistrychemistrySaccharomycetalesElectrophoresis Polyacrylamide GelArchives of Microbiology
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Cell wall mannoproteins during the population growth phases in Saccharomyces cerevisiae.

1987

Mannoproteins from cell walls of Saccharomyces cerevisiae synthesized at successive stages of the population growth cycle have been solubilized with Zymolyase and subsequently analyzed. The major change along the population cycle concerned a large size mannoprotein material; the size of the newly-synthesized molecules varied from 120,000–500,000 (mean of about 200,000) at early exponential phase to 250,000–350,000 (mean of about 300,000) at late exponential phase. These differences are due to modifications in the amount of N-glycosidically linked mannose residues, since the size of the peptide moiety was 90,000–100,000 at all growth stages and the level of O-glycosylation changed only sligh…

GlycosylationSaccharomyces cerevisiaeMannosePeptideSaccharomyces cerevisiaeBiologyBiochemistryMicrobiologylaw.inventionCell wallFungal Proteinschemistry.chemical_compoundlawCell WallGeneticsConcanavalin AMolecular BiologyIncubationGlucanGlycoproteinschemistry.chemical_classificationMembrane GlycoproteinsGlucan Endo-13-beta-D-GlucosidaseSodium Dodecyl SulfateGeneral Medicinebiology.organism_classificationcarbohydrates (lipids)Molecular WeightDithiothreitolMicroscopy ElectronchemistryBiochemistryConcanavalin AFerritinsbiology.proteinChromatography GelElectrophoresis Polyacrylamide GelElectron microscopeArchives of microbiology
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