Search results for "Saccharomyce"

showing 10 items of 875 documents

Transglutaminase activity is involved in Saccharomyces cerevisiae wall construction

2002

Transglutaminase activity, which forms the interpeptidic cross-link N(epsilon)-(gamma-glutamyl)-lysine, was demonstrated in cell-free extracts of Saccharomyces cerevisiae by incorporation of [(14)C]lysine into an exogenous acceptor, N,N'-dimethylcasein. Higher levels of the activity were present in the cell wall, which also contained endogenous acceptors. The enzyme activity in the wall was inhibited by cystamine, a known inhibitor of transglutaminase, and by EDTA, indicating a cation-dependent activity. After the endogenous wall acceptors were labelled radioactively by transglutaminase, extraction with SDS solubilized about 50% of the total radioactivity, while Zymolyase and chitinase each…

Cell ExtractsTransglutaminasesbiologyChemistryTissue transglutaminaseGlucan Endo-13-beta-D-GlucosidaseLysineProtoplastsLysineSaccharomyces cerevisiaeCystamineSaccharomyces cerevisiaebiology.organism_classificationMicrobiologyEnzyme assayYeastCell wallchemistry.chemical_compoundBiochemistryCell WallCystamineChitinasebiology.proteinMicrobiology
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The glucose-dependent transport of L-malate in Zygosaccharomyces bailii.

1984

Zygosaccharomyces bailii possesses a constitutive malic enzyme, but only small amounts of malate are decomposed when the cells ferment fructose. Cells growing anaerobically on glucose (glucose cells) decompose malate, whereas fructose cells do not. Only glucose cells show an increase in the intracellular concentration of malate when suspended in a malate-containing solution. The transport system for malate is induced by glucose, but it is repressed by fructose. The synthesis of this transport system is inhibited by cycloheximide. Of the two enantiomers L-malate is transported preferentially. The transport of malate by induced cells is not only inhibited by addition of fructose but also inac…

Cell Membrane PermeabilityZygosaccharomyces bailiiMalic enzymeMalatesFructoseCycloheximideCarbohydrate metabolismBiologyMicrobiologyMalate dehydrogenaseDiffusionchemistry.chemical_compoundSaccharomycesMolecular BiologyTemperatureFructoseBiological TransportGeneral MedicineMembrane transportbiology.organism_classificationYeastGlucosechemistryBiochemistryFermentationCarrier ProteinsAntonie van Leeuwenhoek
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Evidence for a selective and electroneutral K+/H+-exchange in Saccharomyces cerevisiae using plasma membrane vesicles

1996

The existence of a K+/H+ transport system in plasma membrane vesicles from Saccharomyces cerevisiae is demonstrated using fluorimetric monitoring of proton fluxes across vesicles (ACMA fluorescence quenching). Plasma membrane vesicles used for this study were obtained by a purification/reconstitution protocol based on differential and discontinuous sucrose gradient centrifugations followed by an octylglucoside dilution/gel filtration procedure. This method produces a high percentage of tightly-sealed inside-out plasma membrane vesicles. In these vesicles, the K+/H+ transport system, which is able to catalyse both K+ influx and efflux, is mainly driven by the K+ transmembrane gradient and ca…

Cell Membrane Permeability[SDV]Life Sciences [q-bio]Coated VesiclesCoated vesicleBiological Transport ActiveBioengineeringSaccharomyces cerevisiaeBiologyH(+)-K(+)-Exchanging ATPaseApplied Microbiology and BiotechnologyBiochemistryMembrane PotentialsCell membraneElectron Transport Complex IVH(+)-K(+)-Exchanging ATPasealpha-MannosidaseMannosidasesGeneticsmedicineCentrifugation Density GradientNa+/K+-ATPaseComputingMilieux_MISCELLANEOUSMembrane potentialVesicleCell MembraneDithiazanineElectron Transport Complex IVIsoxazolesHydrogen-Ion ConcentrationMembranemedicine.anatomical_structureSpectrometry Fluorescence[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyBiochemistryBiophysicsChromatography GelPotassiumProtonsMannoseBiotechnology
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Assessing Chronological Aging in Saccharomyces cerevisiae

2012

Saccharomyces cerevisiae is one of the most studied model organisms for the identification of genes and mechanisms that affect aging. The chronological lifespan (CLS) assay, which monitors the survival of a non-dividing population, is one of the two methods to study aging in yeast. To eliminate potential artifacts and identify genes and signaling pathways that may also affect aging in higher eukaryotes, it is important to determine CLS by multiple methods. Here, we describe these methods as well as the assays to study macromolecular damage during aging in yeast, with a focus on genomic instability.

Cell NucleusGenome instabilityGeneticsMutation rateeducation.field_of_studyTime Factorsbiologyved/biologySaccharomyces cerevisiaeved/biology.organism_classification_rank.speciesPopulationFungal geneticsWaterSaccharomyces cerevisiaebiology.organism_classificationArticleGenomic InstabilityYeastCulture Mediayeast genetics aging chronological agingMutation RateDNA FungalModel organismeducationGene
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Subcellular localization and nucleosome specificity of yeast histone acetyltransferases

1991

We have previously reported [López-Rodas et al. (1989) J. Biol. Chem. 264, 19028-19033] that the yeast Saccharomyces cerevisiae contains four histone acetyltransferases, which can be resolved by ion-exchange chromatography, and their specificity toward yeast free histones was studied. In the present contribution we show that three of the enzymes are nuclear, type A histone acetyltransferases and they are able to acetylate nucleosome-bound histones. They differ in their histone specificity. Enzyme A1 acetylates H2A in chicken nucleosomes, although it is specific for yeast free H2B; histone acetyltransferase A2 is highly specific for H3, and histone acetyltransferase A3 preparations acetylate…

Cell NucleusHistone AcetyltransferasesSaccharomyces cerevisiae ProteinsbiologySaccharomyces cerevisiaeHistone acetyltransferaseChromatography Ion ExchangeBiochemistryAmidohydrolasesNucleosomesSubstrate SpecificityHistonesBiochemistryHistone H1AcetyltransferasesHistone methylationHistone H2Abiology.proteinHistone codeHistone octamerHistone deacetylase activityHistone AcetyltransferasesBiochemistry
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Properties of the yeast nuclear histone deacetylase.

1994

A nuclear histone deacetylase from yeast was partially purified and some of its characteristics were studied. Histone deacetylase activity was stimulated in vitro by high-mobility-group nonhistone chromatin proteins 1 and 2 and ubiquitin and inhibited by spermine and spermidine, whereas n-butyrate had no significant inhibitory effect. Like the mammalian enzyme, partially purified histone deacetylase from yeast was strongly inhibited by trichostatin A. However, in crude extract preparations the yeast enzyme was not inhibited and treatment with trichostatin in vivo did not show any effect, either on the histone acetylation level or on cell viability. At low ionic strength, the enzyme can be i…

Cell NucleusHistone deacetylase 5HDAC11ChemistryHistone deacetylase 2HDAC10Cell BiologySaccharomyces cerevisiaeHydroxamic AcidsBiochemistryHistone DeacetylasesSubstrate SpecificityHistone Deacetylase InhibitorsMolecular WeightTrichostatin ABiochemistrymedicineChromatography GelHistone deacetylase activityHistone deacetylaseMolecular Biologymedicine.drugDeacetylase activityResearch ArticleThe Biochemical journal
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Yeast mRNA cap-binding protein Cbc1/Sto1 is necessary for the rapid reprogramming of translation after hyperosmotic shock.

2011

Global translation is inhibited in Saccharomyces cerevisiae cells under osmotic stress; nonetheless, osmostress-protective proteins are synthesized. We found that translation mediated by the mRNA cap-binding protein Cbc1 is stress-resistant and necessary for the rapid translation of osmostress-protective proteins under osmotic stress.

Cell PhysiologySaccharomyces cerevisiae ProteinsOsmotic shockRNA StabilitySaccharomyces cerevisiaeCycloheximideBiology03 medical and health scienceschemistry.chemical_compoundGene Knockout TechniquesEukaryotic translationOsmotic PressureStress PhysiologicalPolysomeGene Expression Regulation FungalProtein biosynthesisRNA MessengerMolecular Biology030304 developmental biologyCell Nucleus0303 health sciencesMicrobial ViabilityOsmotic concentration030302 biochemistry & molecular biologyEIF4ENuclear ProteinsTranslation (biology)Cell BiologyArticlesAdaptation PhysiologicalProtein TransportEukaryotic Initiation Factor-4EchemistryBiochemistryRNA Cap-Binding ProteinsPolyribosomesProtein BiosynthesisProtein BindingMolecular biology of the cell
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Mixed-ligand copper(ii)–sulfonamide complexes: effect of the sulfonamide derivative on DNA binding, DNA cleavage, genotoxicity and anticancer activity

2013

Four ternary complexes, [Cu(L1)2(bipy)] (1) [HL1 = N-(6-chlorobenzo[d]thiazol-2-yl)-4-methylbenzenesulfonamide], [Cu(L2)2(bipy)] (2) [HL2 = N-(benzo[d]thiazol-2-yl)-4-methylbenzenesulfonamide], [Cu(L3)2(bipy)]·1/2H2O (3) [HL3 = N-(5,6-dimethylbenzo[d]thiazol-2-yl)-4-methylbenzenesulfonamide] and [Cu(L4)2(bipy)] (4) [HL4 = N-(5,6-dimethylbenzo[d]thiazol-2-yl)benzenesulfonamide], were prepared and then characterized by X-ray crystallography, spectroscopy and magnetic measurements. Whereas the molecular structure of 1 and 2 consists of a discrete monomeric copper(II) species with a distorted square planar geometry, that of 3 and 4 consists of two independent molecules. In 3, both molecules pre…

Cell SurvivalStereochemistryDNA damageAntineoplastic AgentsApoptosisSaccharomyces cerevisiaeLigandsInorganic ChemistryJurkat Cellschemistry.chemical_compoundCoordination ComplexesHumansMoleculeDNA CleavageCell ProliferationCoordination geometrychemistry.chemical_classificationSulfonamidesDNASquare pyramidal molecular geometryIn vitroSulfonamideCrystallographyMonomerchemistryCaco-2 CellsCopperDNADalton Transactions
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The yeast mitogen-activated protein kinase Slt2 is involved in the cellular response to genotoxic stress

2012

Abstract Background The maintenance of genomic integrity is essential for cell viability. Complex signalling pathways (DNA integrity checkpoints) mediate the response to genotoxic stresses. Identifying new functions involved in the cellular response to DNA-damage is crucial. The Saccharomyces cerevisiae SLT2 gene encodes a member of the mitogen-activated protein kinase (MAPK) cascade whose main function is the maintenance of the cell wall integrity. However, different observations suggest that SLT2 may also have a role related to DNA metabolism. Results This work consisted in a comprehensive study to connect the Slt2 protein to genome integrity maintenance in response to genotoxic stresses.…

Cell cycle checkpoint<it>Saccharomyces cerevisiae</it>DNA damageSaccharomyces cerevisiaeGenotoxic StressSaccharomyces cerevisiaeBiologyBiochemistrylcsh:RC254-282checkpointlcsh:QH573-671Protein kinase AMolecular BiologyGeneticsDNA integrity checkpointKinaselcsh:CytologyResearchCell BiologyCell cyclebiology.organism_classificationlcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensgenotoxic stressCell biologyDNA damageSlt2
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Adenine auxotrophy--be aware: some effects of adenine auxotrophy in Saccharomyces cerevisiae strain W303-1A.

2013

Adenine auxotrophy is a commonly used genetic marker in haploid yeast strains. Strain W303-1A, which carries the ade2-1 mutation, is widely used in physiological and genetic research. Yeast extract-based rich medium contains a low level of adenine, so that adenine is often depleted before glucose. This could affect the cell physiology of adenine auxotrophs grown in rich medium. The aim of our study was to assess the effects of adenine auxotrophy on cell morphology and stress physiology. Our results show that adenine depletion halts cell division, but that culture optical density continues to increase due to cell swelling. Accumulation of trehalose and a coincident 10-fold increase in desicc…

Cell physiologyCell divisionAuxotrophyAdenineSaccharomyces cerevisiaeGeneral MedicineSaccharomyces cerevisiaeBiologybiology.organism_classificationCell morphologyApplied Microbiology and BiotechnologyMicrobiologyTrehaloseYeastCulture Mediachemistry.chemical_compoundBiochemistrychemistryStress PhysiologicalBiomassLeucineCell DivisionFEMS yeast research
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