Search results for "Saccharomyces cerevisiae Proteins"

showing 10 items of 231 documents

Evolution of osmosensing signal transduction in Metazoa: stress-activated protein kinases p38 and JNK.

2001

Sponges (Porifera) represent the most basal branch of the Metazoa alive today. We show that two central stress-activated protein kinases involved in the osmosensing pathway, p38 mitogen-activated protein kinase (MAPK) and JNK, can complement for the ancestral MAPK Hog1 in the yeast Saccharomyces cerevisiae. S. cerevisiae mutants lacking Hog1 (hog1-Delta 1) have been complemented with the sponge SDJNK and SDp38 genes. Western blotting has revealed that, after transformation, the hog1-Delta 1+ SDJNK(sense) and hog1-Delta 1+ SDp38(sense) clones express the sponge proteins. Functional studies have demonstrated that the complemented clones grow under hyperosmotic conditions (0.6 M NaCl). Further…

MAPK/ERK pathwayxHistologySaccharomyces cerevisiae ProteinsMAP Kinase Kinase 4p38 mitogen-activated protein kinasesSaccharomyces cerevisiaeMutantSaccharomyces cerevisiaeSodium Chloridep38 Mitogen-Activated Protein KinasesPathology and Forensic MedicineTransformation GeneticOsmotic PressureAnimalsMitogen-Activated Protein Kinase 8PhosphorylationProtein kinase APhylogenyMitogen-Activated Protein Kinase KinasesbiologyKinaseJNK Mitogen-Activated Protein KinasesCell BiologyWater-Electrolyte Balancebiology.organism_classificationCell biologyPoriferaPhosphorylationSignal transductionMitogen-Activated Protein KinasesSignal TransductionCell and tissue research
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Genetic elimination of known pheromones reveals the fundamental chemical bases of mating and isolation in Drosophila

1999

Overexpression of the UAS-tra transgene in Drosophila melanogaster females led to the complete elimination of their cuticular pheromones. According to current models of Drosophila behavior, these flies should induce no courtship. In fact, they are still attractive to conspecific males. Three classes of stimuli are shown to induce courtship, with different effects on male behavior: ( i ) known pheromones produced by control females, ( ii ) stimuli produced by living control and transgenic flies, and ( iii ) as-yet-undetermined pheromones present on both control and transgenic flies. Only the latter class of pheromones are required for mating. They appear to represent a layer of ancestral at…

MaleHot TemperaturePheromones/genetics/*physiologyPheromonesAnimals Genetically ModifiedCourtshipSexual Behavior AnimalAnimal/*physiologyMelanogasterMatingreproductive and urinary physiologymedia_commonGeneticsMultidisciplinarybiologyBiological SciencesDNA-Binding ProteinsDrosophila melanogasterSocial IsolationSex pheromonebehavior and behavior mechanismsDrosophilaFemaleDrosophila melanogasteranimal structuresSaccharomyces cerevisiae ProteinsGenotypeRecombinant Fusion ProteinsRecombinant Fusion Proteins/biosynthesisSexual BehaviorTransgenemedia_common.quotation_subjectGenetically ModifiedCrossesHSP70 Heat-Shock Proteins/biosynthesis/genetics/physiologyFungal ProteinsGeneticSibling speciesAnimalsHSP70 Heat-Shock ProteinsDrosophilaCrosses Geneticfungibiology.organism_classificationHeatTranscription Factors/biosynthesis/geneticsFungal Proteins/biosynthesis/geneticsHydrocarbonsDrosophila melanogaster/genetics/*physiologyEvolutionary biologyDrosophila/genetics/*physiologyTranscription FactorsProceedings of the National Academy of Sciences
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Genetic identification of neurons controlling a sexually dimorphic behaviour

2000

0960-9822 (Print) Journal Article Research Support, Non-U.S. Gov't; In the fruit fly Drosophila melanogaster, locomotor activity is sexually dimorphic: female flies constantly modulate their activity pattern whereas males show a steadier, stereotyped walking pace [1]. Here, we mapped the area of the brain controlling this behavioural dimorphism. Adult male Drosophila expressing a dominant feminising transgene in a small cluster of neurons in the pars intercerebralis exhibited a female-like pattern of locomotor activity. Genetic ablation of these neurons prevented the feminisation of the locomotor activity of transgenic males. The results suggest that this cluster of neurons modulates sex-sp…

MaleMESH: NeuronsCourtshipAnimals Genetically ModifiedSexual Behavior Animal0302 clinical medicineMESH: Saccharomyces cerevisiae ProteinsDrosophila ProteinsNervous System Physiological PhenomenaMESH: AnimalsMESH: Sexual Behavior AnimalDrosophila melanogaster/*physiologymedia_commonNeurons0303 health sciencesFungal proteinSex CharacteristicsbiologyAgricultural and Biological Sciences(all)Nuclear ProteinsAnatomyMESH: Transcription FactorsMotor Activity/*physiologyMESH: Motor ActivityDNA-Binding ProteinsFungal Proteins/geneticsNuclear Proteins/*genetics/physiologyDrosophila melanogasterMESH: Fungal Proteins[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]FemaleDrosophila melanogasterGeneral Agricultural and Biological SciencesLocomotionSex characteristicsMESH: Sex CharacteristicsNervous System PhysiologySaccharomyces cerevisiae ProteinsTransgenemedia_common.quotation_subjectRecombinant Fusion ProteinsRecombinant Fusion Proteins/biosynthesisSexual BehaviorMESH: LocomotionTranscription Factors/geneticsGenetically ModifiedMotor ActivityGeneral Biochemistry Genetics and Molecular BiologyMESH: Drosophila melanogasterFungal ProteinsMESH: Animals Genetically Modified03 medical and health sciencesMESH: Recombinant Fusion ProteinsAnimalsDrosophila030304 developmental biologyBiochemistry Genetics and Molecular Biology(all)Animalfungibiology.organism_classificationMESH: MaleSexual dimorphismMale courtship behaviourMESH: Nervous System PhysiologyNeuroscienceMESH: FemaleMESH: Nuclear ProteinsNeurons/*physiology030217 neurology & neurosurgeryTranscription Factors
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Convergent adaptation of Saccharomyces uvarum to sulfite, an antimicrobial preservative widely used in human-driven fermentations

2021

Different species can find convergent solutions to adapt their genome to the same evolutionary constraints, although functional convergence promoted by chromosomal rearrangements in different species has not previously been found. In this work, we discovered that two domesticated yeast species, Saccharomyces cerevisiae, and Saccharomyces uvarum, acquired chromosomal rearrangements to convergently adapt to the presence of sulfite in fermentation environments. We found two new heterologous chromosomal translocations in fermentative strains of S. uvarum at the SSU1 locus, involved in sulfite resistance, an antimicrobial additive widely used in food production. These are convergent events that …

Metabolic ProcessesCancer ResearchAdaptation BiologicalYeast and Fungal ModelsArtificial Gene Amplification and ExtensionWineChromosomal translocationQH426-470BiochemistryGenomeTranslocation Geneticchemistry.chemical_compoundAnti-Infective AgentsMedicine and Health SciencesPromoter Regions GeneticPhylogenyGenetics (clinical)GeneticsChromosome BiologyAlcoholic BeveragesEukaryotaGenomicsChromosomal AberrationsPolymerase chain reactionChemistryExperimental Organism SystemsPhysical SciencesChromosomes FungalResearch ArticleSaccharomyces cerevisiae ProteinsAnion Transport ProteinsSaccharomyces cerevisiaeLocus (genetics)Saccharomyces cerevisiaeChromosomal translocationsBiologyResearch and Analysis MethodsBeveragesSaccharomycesModel OrganismsSulfiteGeneticsHumansSulfitesMolecular Biology TechniquesMolecular BiologyGeneEcology Evolution Behavior and SystematicsNutritionChemical CompoundsOrganismsFungiBiology and Life SciencesCell Biologybiology.organism_classificationYeastYeastDietMetabolismchemistryFermentationFood PreservativesAnimal StudiesAdaptationPLOS Genetics
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FICC-Seq: a method for enzyme-specified profiling of methyl-5-uridine in cellular RNA.

2019

AbstractMethyl-5-uridine (m5U) is one the most abundant non-canonical bases present in cellular RNA, and in yeast is found at position U54 of tRNAs where modification is catalysed by the methyltransferase Trm2. Although the mammalian enzymes that catalyse m5U formation are yet to be identified via experimental evidence, based on sequence homology to Trm2, two candidates currently exist, TRMT2A and TRMT2B. Here we developed a genome-wide single-nucleotide resolution mapping method, Fluorouracil-Induced-Catalytic-Crosslinking-Sequencing (FICC-Seq), in order to identify the relevant enzymatic targets. We demonstrate that TRMT2A is responsible for the majority of m5U present in human RNA, and t…

MethyltransferaseSaccharomyces cerevisiae ProteinsCell SurvivalSaccharomyces cerevisiaeBiology03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA TransferYeastsGeneticsHumansNucleotideUridine030304 developmental biologychemistry.chemical_classification0303 health sciencestRNA MethyltransferasesDeoxyribonucleasesHEK 293 cellsRNAHigh-Throughput Nucleotide SequencingYeastUridineEnzymeHEK293 CellsBiochemistrychemistry030220 oncology & carcinogenesisTransfer RNARNAMethods OnlineFluorouracilNucleic acids research
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Transcriptional expression of selected genes associated with excretion of carboxylic acids from aci mutants of Saccharomyces cerevisiae

2013

Introduction: Saccharomyces cerevisiae is an excellent model organism for studies of transcriptional regulation of metabolic processes in other eukaryotic cells including human cells. Cellular acid-base balance can be disturbed in pathologic situations such as renal acidosis or cancer. The extracellular pH of malignant solid tumors is acidic in the range of 6.5-6.9. EG07 and EG37 aci mutants of Saccharomyces cerevisiae excessively excrete carboxylic acids to glucose-containing media or distilled water. The excreted acids are Krebs and/or glyoxylate cycle intermediates. The genes restoring the wild-type phenotype have function that does not easily explain theAci phenotype.Material/Methods: I…

Microbiology (medical)Transcriptional ActivationSaccharomyces cerevisiae ProteinsCarboxylic acidKrebs and glyoxylate cycleMutantSaccharomyces cerevisiaeCitric Acid CycleGlyoxylate cycleCarboxylic AcidsGene Expressionlcsh:MedicineSaccharomyces cerevisiaeBiologyaci mutantsSpecies SpecificityTranscriptional regulationHumansRNA MessengerGenechemistry.chemical_classificationacid transporterslcsh:RGlyoxylatesMembrane Transport ProteinsBiological Transportbiology.organism_classificationMolecular biologyPhenotypeCitric acid cycleProton-Translocating ATPasesInfectious DiseasesGlucoseBiochemistrychemistryMutationATP-Binding Cassette TransportersPostępy Higieny i Medycyny Doświadczalnej
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Yeast Translation Elongation Factor eIF5A Expression Is Regulated by Nutrient Availability through Different Signalling Pathways

2020

Translation elongation factor eIF5A binds to ribosomes to promote peptide bonds between problematic amino acids for the reaction like prolines. eIF5A is highly conserved and essential in eukaryotes, which usually contain two similar but differentially expressed paralogue genes. The human eIF5A-1 isoform is abundant and implicated in some cancer types

MitochondrionBiotecnologialcsh:ChemistryPeptide Initiation FactorsGene Expression Regulation Fungalmitochondrial respirationGene expressionExpressió genèticaHap1Protein Isoformshemelcsh:QH301-705.5SpectroscopyChemistryRNA-Binding ProteinsTranslation (biology)Iron DeficienciesGeneral MedicineTORAerobiosisUp-RegulationComputer Science ApplicationsCell biologySnf1EIF5ASignal TransductionGene isoformSaccharomyces cerevisiae ProteinsIronCitric Acid CycleDown-RegulationSaccharomyces cerevisiaeMechanistic Target of Rapamycin Complex 1Models BiologicalArticleCatalysisInorganic ChemistryeIF5APhysical and Theoretical ChemistryMolecular BiologyTranscription factorGeneLysineOrganic ChemistryNutrientsMetabolismCarbonMetabolic Flux AnalysisGlucoselcsh:Biology (General)lcsh:QD1-999Fermentationgene expressionInternational Journal of Molecular Sciences
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The Protein Structure Context of PolyQ Regions.

2016

Proteins containing glutamine repeats (polyQ) are known to be structurally unstable. Abnormal expansion of polyQ in some proteins exceeding a certain threshold leads to neurodegenerative disease, a symptom of which are protein aggregates. This has led to extensive research of the structure of polyQ stretches. However, the accumulation of contradictory results suggests that protein context might be of importance. Here we aimed to evaluate the structural context of polyQ regions in proteins by analysing the secondary structure of polyQ proteins and their homologs. The results revealed that the secondary structure in polyQ vicinity is predominantly random coil or helix. Importantly, the region…

Models MolecularProtein Conformation alpha-HelicalProtein Structure ComparisonProtein StructureSaccharomyces cerevisiae ProteinsGlutaminelcsh:MedicineNerve Tissue ProteinsSaccharomyces cerevisiaePlant ScienceResearch and Analysis MethodsBiochemistryPlant Roots570 Life sciencesDatabase and Informatics MethodsProtein Structure DatabasesMacromolecular Structure AnalysisHumansProtein Interaction Domains and MotifsAmino AcidsDatabases ProteinProtein Interactionslcsh:ScienceMolecular BiologyMediator ComplexOrganic CompoundsPlant AnatomyAcidic Amino AcidsOrganic Chemistrylcsh:RChemical CompoundsBiology and Life SciencesProteinsRoot StructureChemistryBiological DatabasesProtein-Protein InteractionsPhysical Scienceslcsh:QStructural ProteinsProtein Structure DeterminationPeptidesResearch Article570 BiowissenschaftenPLoS ONE
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Structural Characterization of Set1 RNA Recognition Motifs and their Role in Histone H3 Lysine 4 Methylation

2006

Departament de Bioquimica iBiologia Molecular, Universitatde Valencia, C/Dr Moliner 50,46100, Burjassot, SpainThe yeast Set1 histone H3 lysine 4 (H3K4) methyltransferase contains, inaddition to its catalytic SET domain, a conserved RNA recognition motif(RRM1). We present here the crystal structure and the secondary structureassignment in solution of the Set1 RRM1. Although RRM1 has the expectedβαββαβ RRM-fold, it lacks the typical RNA-binding features of thesemodules. RRM1 is not able to bind RNA by itself in vitro, but a constructcombining RRM1 with a newly identified downstream RRM2 specificallybinds RNA. Invivo,H3K4 methylation isnot affectedbyapoint mutation inRRM2 that preserves Set1 s…

Models MolecularRiboswitchHistone H3 Lysine 4Saccharomyces cerevisiae ProteinsRNA-induced transcriptional silencingSurface Properties[SDV]Life Sciences [q-bio]Molecular Sequence DataSaccharomyces cerevisiae[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]BiologyMethylationHistonesStructure-Activity Relationship03 medical and health sciencesStructural BiologyHistone methylation[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Amino Acid SequenceProtein Structure QuaternaryMolecular BiologyConserved Sequence030304 developmental biology0303 health sciencesRNA recognition motifLysine030302 biochemistry & molecular biologyRNARNA FungalHistone-Lysine N-MethyltransferaseNon-coding RNAMolecular biology[SDV] Life Sciences [q-bio]DNA-Binding ProteinsProtein SubunitsBiochemistryHistone methyltransferaseSequence AlignmentProtein BindingTranscription Factors
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Structures of yeast peroxisomal Δ(3),Δ(2)-enoyl-CoA isomerase complexed with acyl-CoA substrate analogues: the importance of hydrogen-bond networks f…

2015

Δ3,Δ2-Enoyl-CoA isomerases (ECIs) catalyze the shift of a double bond from 3Z- or 3E-enoyl-CoA to 2E-enoyl-CoA. ECIs are members of the crotonase superfamily. The crotonase framework is used by many enzymes to catalyze a wide range of reactions on acyl-CoA thioesters. The thioester O atom is bound in a conserved oxyanion hole. Here, the mode of binding of acyl-CoA substrate analogues to peroxisomalSaccharomyces cerevisiaeECI (ScECI2) is described. The best defined part of the bound acyl-CoA molecules is the 3′,5′-diphosphate-adenosine moiety, which interacts with residues of loop 1 and loop 2, whereas the pantetheine part is the least well defined. The catalytic base, Glu158, is hydrogen-bo…

Models MolecularSaccharomyces cerevisiae ProteinsDouble bondStereochemistryProtein ConformationIsomeraseSaccharomyces cerevisiaeEnoyl CoA isomeraseThioesterPhotochemistryDodecenoyl-CoA Isomerasebeta-oxidationSubstrate SpecificityStructural Biologyddc:570Catalytic DomainEnzyme StabilitySide chainMoietyta116chemistry.chemical_classificationHydrogen bondenoyl-CoA isomeraseta1182Hydrogen BondingGeneral Medicinehydrogen-bond networkcrotonaseoxyanion holechemistryAcyl Coenzyme AOxyanion holeOxidation-ReductionProtein BindingActa crystallographica. Section D, Biological crystallography
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