Search results for "Saccharomyce"

showing 10 items of 875 documents

Enhanced antifungal efficacy of tebuconazole using gated pH-driven mesoporous nanoparticles

2014

Núria Mas,1–3 Irene Galiana,3 Silvia Hurtado,† Laura Mondragón,1–3 Andrea Bernardos,1–3 Félix Sancenón,1–3 María D Marcos,1–3 Pedro Amorós,4 Nuria Abril-Utrillas,5 Ramón Martínez-Máñez,1–3 José Ramón Murguía1,3 1Centro de Reconocimiento Molecular y Desarrollo Tecnológico (IDM), Centro Mixto Universidad Politécnica de Valencia, Universidad de Valencia, Valencia, Spain; 2Departamento de Química, Universidad Politécnica de Valencia, Valenci…

INGENIERIA DE LA CONSTRUCCIONMaterials scienceAntifungal AgentsPH-responsive nanoparticlesCell Survivalmedia_common.quotation_subjectCapped mesoporous nanoparticlesBiophysicsPharmaceutical ScienceNanoparticleBioengineeringSaccharomyces cerevisiaeNanocapsulesBiomaterialsDiffusionchemistry.chemical_compoundNanoporesQUIMICA ORGANICANanocapsulesInternational Journal of NanomedicineDrug DiscoveryQUIMICA ANALITICABIOQUIMICA Y BIOLOGIA MOLECULARFluoresceinParticle SizeCytotoxicityInternalizationmedia_commonTebuconazoleOriginal ResearchIntracellular releaseOrganic ChemistryQUIMICA INORGANICADrug SynergismGeneral MedicineMesoporous silicaHydrogen-Ion ConcentrationTriazoleschemistryBiochemistryDelayed-Action PreparationsBiophysicsTebuconazole loadingMesoporous materialPorosityInternational Journal of Nanomedicine
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Structure and function of the vacuolar Ccc1/VIT1 family of iron transporters and its regulation in fungi

2020

Iron is an essential micronutrient for most living beings since it participates as a redox active cofactor in many biological processes including cellular respiration, lipid biosynthesis, DNA replication and repair, and ribosome biogenesis and recycling. However, when present in excess, iron can participate in Fenton reactions and generate reactive oxygen species that damage cells at the level of proteins, lipids and nucleic acids. Organisms have developed different molecular strategies to protect themselves against the harmful effects of high concentrations of iron. In the case of fungi and plants, detoxification mainly occurs by importing cytosolic iron into the vacuole through the Ccc1/V…

ISC Iron-sulfur lusterCS Consistency scoreCcc1Ribosome biogenesisVacuoleReview ArticleYRE Yap response elementsBiochemistryBiotecnologia0302 clinical medicineStructural BiologyCg Candida glabrata0303 health sciencesMAFFT Multiple Alignment using Fast Fourier TransformNRAMP Natural Resistance-Associated Macrophage ProteinbiologyVIT1ChemistryMBD Metal-binding domainPlantsComputer Science ApplicationsBiochemistry030220 oncology & carcinogenesisCRD Cysteine-rich domainEg Eucalyptus grandisIron detoxificationBiotechnologyCBC CCAAT-binding core complexlcsh:BiotechnologySaccharomyces cerevisiaeVTL Vacuolar iron transporter-likeBiophysicsVIT Vacuolar iron transporterbZIP basic leucine-zipper03 medical and health sciencesFongsLipid biosynthesislcsh:TP248.13-248.65GeneticsFe IronIron transportTranscription factor030304 developmental biologyComputingMethodologies_COMPUTERGRAPHICSBLOSUM BLOcks SUbstitution MatrixTMD Transmembrane domainML Maximum-likelihoodIron regulationDNA replicationFungibiology.organism_classificationYeastYeastMetabolic pathwayH HelixHap Heme activator proteinVacuoleROS Reactive oxygen speciesFerroComputational and Structural Biotechnology Journal
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Yeast ecology of vineyards within Marsala wine area (western Sicily) in two consecutive vintages and selection of autochthonous Saccharomyces cerevis…

2012

In this work, the yeast ecology associated with the spontaneous fermentation of Grillo cultivar grapes from 10 vineyards was analyzed from grape harvest till complete consumption of must sugars. The microbiological investigation started with the plate count onto two culture media to distinguish total yeasts (TY) and presumptive Saccharomyces (PS). Yeasts were randomly isolated and identified by a combined genotypic approach consisting of restriction fragment length polymorphism (RFLP) of 5.8S rRNA gene and 26S rRNA and sequencing of D1/D2 domain of the 26S rRNA gene, which resulted in the recognition of 14 species belonging to 10 genera. The distribution of the yeasts within the vineyards s…

IdentificationGenotypeSaccharomyces cerevisiaeAcetic Acid; Culture Media; DNA Fungal; Ethanol; Fermentation; Genotype; Hydrogen Sulfide; Microsatellite Repeats; Polymerase Chain Reaction; Polymorphism Restriction Fragment Length; RNA Ribosomal; Saccharomyces cerevisiae; Sicily; Sulfites; Temperature; Vitis; WineBioengineeringWineSaccharomyces cerevisiaeBiologyApplied Microbiology and BiotechnologySaccharomycesPolymerase Chain ReactionEnological aptitudeYeastsGenotypeSulfitesVitisHydrogen SulfidePolymorphismDNA FungalSicilyAcetic AcidRibosomalWineEthanolEcologyIdentification; Enological aptitudes; Saccharomyces cerevisiae; Spontaneous wine fermentation; YeastsTemperatureDNARibosomal RNASpontaneous wine fermentationbiology.organism_classificationYeastCulture MediaFungalRestriction Fragment LengthRNA RibosomalFermentationRNAFermentationRestriction fragment length polymorphismPolymorphism Restriction Fragment LengthBiotechnologySettore AGR/16 - Microbiologia AgrariaMicrosatellite RepeatsJournal of bioscience and bioengineering
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Presence and coding properties of 2'-O-methyl-5-carbamoylmethyluridine (ncm5Um) in the wobble position of the anticodon of tRNA(Leu) (U*AA) from brew…

1992

AbstractThe unknown modified nucleoside U* has been isolated by enzymatic and HPLC protocols from tRNALeu(U*AA) recently discovered in brewer's yeast. The pure U* nucleoside has been characterized by electron impact mass spectroscopy, and comparison of its chromatographic and UV-absorption properties with those of appropriate synthetic compounds. The structure of U* was established as 2′-O-methyl-5-carbamoylmethyluridine (ncm5Um). The yeast tRNALeu (U*AA) is the only tRNA so far sequenced which has been shown to contain ncm5Um. The location of such a modified uridine at the first position of the anticodon restricts the decoding property to A of the leucine UUA codon.

IdentificationRNA Transfer LeuStereochemistryBiophysicsAminoacylationWobble base pairModified nucleosideSaccharomyces cerevisiaeBiochemistryMass SpectrometryFungal Proteinschemistry.chemical_compoundStructural BiologyGeneticsAnticodonMolecular BiologyUridineChromatography High Pressure Liquidchemistry.chemical_classificationMolecular StructureRNA FungalCell BiologyUridineYeastYeastEnzymechemistryBiochemistryTransfer RNAtRNALeu (U*AA)Spectrophotometry UltravioletLeucineNucleosideFEBS letters
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The glyceraldehyde-3-phosphate dehydrogenase polypeptides encoded by the Saccharomyces cerevisiae TDH1, TDH2 and TDH3 genes are also cell wall protei…

2001

The authors show that the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of Saccharomyces cerevisiae, previously thought to be restricted to the cell interior, is also present in the cell wall. GAPDH activity, proportional to cell number and time of incubation, was detected in intact wild-type yeast cells. Intact cells of yeast strains containing insertion mutations in each of the three structural TDH genes (tdh1, tdh2 and tdh3) and double mutants (tdh1 tdh2 and tdh1 tdh3) also displayed a cell-wall-associated GAPDH activity, in the range of parental wild-type cells, although with significant differences among strains. A cell wall location of GAPDH was further confirmed …

Immunoelectron microscopySaccharomyces cerevisiaeCellBlotting WesternGenes FungalSaccharomyces cerevisiaeBiologyMicrobiologyCell wallstomatognathic systemBacterial ProteinsCell WallmedicineFluorescent Antibody Technique IndirectMicroscopy ImmunoelectronGlyceraldehyde 3-phosphate dehydrogenaseGlyceraldehyde-3-Phosphate Dehydrogenasesbiology.organism_classificationFlow CytometryMolecular biologyYeastCulture MediaCytosolmedicine.anatomical_structureBiochemistryCytoplasmMutationbiology.proteinMicrobiology (Reading, England)
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Protein Kinase C μ Is Regulated by the Multifunctional Chaperon Protein p32

2000

We identified the multifunctional chaperon protein p32 as a protein kinase C (PKC)-binding protein interacting with PKCalpha, PKCzeta, PKCdelta, and PKC mu. We have analyzed the interaction of PKC mu with p32 in detail, and we show here in vivo association of PKC mu, as revealed from yeast two-hybrid analysis, precipitation assays using glutathione S-transferase fusion proteins, and reciprocal coimmunoprecipitation. In SKW 6.4 cells, PKC mu is constitutively associated with p32 at mitochondrial membranes, evident from colocalization with cytochrome c. p32 interacts with PKC mu in a compartment-specific manner, as it can be coimmunoprecipitated mainly from the particulate and not from the so…

ImmunoprecipitationRecombinant Fusion ProteinsGolgi ApparatusSaccharomyces cerevisiaeSpodopteraMitogen-activated protein kinase kinaseBiologyTransfectionBiochemistryCell LineMitochondrial ProteinsAnimalsHumansCloning MolecularKinase activityMolecular BiologyProtein Kinase CProtein kinase CGlutathione TransferaseB-LymphocytesBinding SitesMembrane GlycoproteinsKinaseAutophosphorylationJNK Mitogen-Activated Protein KinasesCell BiologyFusion proteinMitochondriaReceptors ComplementCell biologybody regionsHyaluronan ReceptorsProtein kinase domainBiochemistryMitogen-Activated Protein KinasesCarrier ProteinsMolecular ChaperonesProtein BindingJournal of Biological Chemistry
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A novel target of lithium therapy.

2000

Phosphatases converting 3'-phosphoadenosine 5'-phosphate (PAP) into adenosine 5'-phosphate are of fundamental importance in living cells as the accumulation of PAP is toxic to several cellular systems. These enzymes are lithium-sensitive and we have characterized a human PAP phosphatase as a potential target of lithium therapy. A cDNA encoding a human enzyme was identified by data base screening, expressed in Escherichia coli and the 33 kDa protein purified to homogeneity. The enzyme exhibits high affinity for PAP (K(m)1 microM) and is sensitive to subtherapeutic concentrations of lithium (IC(50)=0.3 mM). The human enzyme also hydrolyzes inositol-1, 4-bisphosphate with high affinity (K(m)=0…

Inositol-14-bisphosphateDNA ComplementaryBicinePhosphataseMolecular Sequence DataBiophysicschemistry.chemical_elementSaccharomyces cerevisiaeLithiummedicine.disease_causeBiochemistrychemistry.chemical_compoundStructural BiologyNucleotidasesComplementary DNAPhosphataseGeneticsmedicineEscherichia coliHumansAmino Acid SequenceCloning MolecularMolecular BiologyEscherichia coliIC50Chromatography High Pressure Liquidchemistry.chemical_classificationExpressed Sequence TagsBase Sequence3′-Phosphoadenosine 5′-phosphateCell BiologyMolecular biologyAdenosineAdenosine MonophosphatePhosphoric Monoester HydrolasesAdenosine DiphosphateEnzymechemistryBiochemistryLithiummedicine.drugHumanFEBS letters
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A genome-wide transcriptional study reveals that iron deficiency inhibits the yeast TORC1 pathway

2019

Iron is an essential micronutrient that participates as a cofactor in a broad range of metabolic processes including mitochondrial respiration, DNA replication, protein translation and lipid biosynthesis. Adaptation to iron deficiency requires the global reorganization of cellular metabolism directed to optimize iron utilization. The budding yeast Saccharomyces cerevisiae has been widely used to characterize the responses of eukaryotic microorganisms to iron depletion. In this report, we used a genomic approach to investigate the contribution of transcription rates to the modulation of mRNA levels during adaptation of yeast cells to iron starvation. We reveal that a decrease in the activity…

IronSaccharomyces cerevisiaeBiophysicsRibosome biogenesisSaccharomyces cerevisiaeMechanistic Target of Rapamycin Complex 1Biochemistry03 medical and health sciencesStructural BiologyRibosomal proteinTranscription (biology)Gene Expression Regulation FungalLipid biosynthesisGeneticsHumansRNA MessengerPhosphorylationMolecular BiologyGene030304 developmental biology0303 health sciencesAnemia Iron-Deficiencybiology030306 microbiologyChemistryIron deficiencyRNA polymerasesRNATORbiology.organism_classificationAdaptation PhysiologicalYeastCell biologyDNA-Binding ProteinsGene Expression RegulationProtein BiosynthesisSignal transductionTranscription
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The elemental role of iron in DNA synthesis and repair

2017

Iron is an essential redox element that functions as a cofactor in many metabolic pathways. Critical enzymes in DNA metabolism, including multiple DNA repair enzymes (helicases, nucleases, glycosylases, demethylases) and ribonucleotide reductase, use iron as an indispensable cofactor to function. Recent striking results have revealed that the catalytic subunit of DNA polymerases also contains conserved cysteine-rich motifs that bind iron–sulfur (Fe/S) clusters that are essential for the formation of stable and active complexes. In line with this, mitochondrial and cytoplasmic defects in Fe/S cluster biogenesis and insertion into the nuclear iron-requiring enzymes involved in DNA synthesis a…

Iron-Sulfur Proteins0301 basic medicineDNA RepairDNA polymeraseDNA damageDNA repairIronBiophysicsDNA repairEukaryotic DNA replicationSaccharomyces cerevisiaeBiochemistryDNA GlycosylasesBiomaterials03 medical and health sciencesRibonucleotide ReductasesHumansProtein–DNA interactionRibonucleotide reductaseReplication protein Achemistry.chemical_classificationDNA ligaseDeoxyribonucleasesDNA synthesis030102 biochemistry & molecular biologybiologyIron deficiencyDNA HelicasesMetals and AlloysHelicaseDNAYeast030104 developmental biologyIron cofactorBiochemistrychemistryChemistry (miscellaneous)biology.proteinIron-sulfur clusterMetallomics
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Yeast Dun1 Kinase Regulates Ribonucleotide Reductase Inhibitor Sml1 in Response to Iron Deficiency

2014

Iron is an essential micronutrient for all eukaryotic organisms because it participates as a redox-active cofactor in many biological processes, including DNA replication and repair. Eukaryotic ribonucleotide reductases (RNRs) are Fe-dependent enzymes that catalyze deoxyribonucleoside diphosphate (dNDP) synthesis. We show here that the levels of the Sml1 protein, a yeast RNR large-subunit inhibitor, specifically decrease in response to both nutritional and genetic Fe deficiencies in a Dun1-dependent but Mec1/Rad53- and Aft1-independent manner. The decline of Sml1 protein levels upon Fe starvation depends on Dun1 forkhead-associated and kinase domains, the 26S proteasome, and the vacuolar pr…

Iron-Sulfur ProteinsProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsDeoxyribonucleoside triphosphateRibonucleotideIronDeoxyribonucleotidesGenes FungalSaccharomyces cerevisiaeCell Cycle ProteinsSaccharomyces cerevisiaeRibonucleotide reductase inhibitorProtein Serine-Threonine KinasesBiologyProtein degradationchemistry.chemical_compoundTristetraprolinRibonucleotide ReductasesAspartic Acid EndopeptidasesPhosphorylationMolecular BiologyCheckpoint Kinase 2Binding SitesKinaseIntracellular Signaling Peptides and ProteinsArticlesCell Biologybiology.organism_classificationDNA-Binding ProteinsDeoxyribonucleosideCheckpoint Kinase 2chemistryBiochemistryProteolysisGene DeletionTranscription FactorsMolecular and Cellular Biology
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