Search results for "Saccharomyces cerevisiae Proteins"

showing 10 items of 231 documents

Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator

2019

Abstract Posttranscriptional RNA modifications occur in all domains of life. Modifications of anticodon bases are of particular importance for ribosomal decoding and proteome homeostasis. The Elongator complex modifies uridines in the wobble position and is highly conserved in eukaryotes. Despite recent insights into Elongator's architecture, the structure and function of its regulatory factor Kti12 have remained elusive. Here, we present the crystal structure of Kti12′s nucleotide hydrolase domain trapped in a transition state of ATP hydrolysis. The structure reveals striking similarities to an O-phosphoseryl-tRNA kinase involved in the selenocysteine pathway. Both proteins employ similar …

TRNA modificationSaccharomyces cerevisiae ProteinsProtein ConformationWobble base pairSaccharomyces cerevisiaeBiologyChaetomiumCrystallography X-Ray03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA TransferATP hydrolysisGeneticsRNA and RNA-protein complexesAnticodonRNA Processing Post-TranscriptionalUridine030304 developmental biologyAdaptor Proteins Signal TransducingAdenosine Triphosphatases0303 health sciencesSelenocysteineRNATRNA bindingCell biologychemistryTransfer RNASelenocysteine incorporationCarrier ProteinsRibosomes030217 neurology & neurosurgery
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Chromatin modifiers and recombination factors promote a telomere fold-back structure, that is lost during replicative senescence.

2020

Telomeres have the ability to adopt a lariat conformation and hence, engage in long and short distance intra-chromosome interactions. Budding yeast telomeres were proposed to fold back into subtelomeric regions, but a robust assay to quantitatively characterize this structure has been lacking. Therefore, it is not well understood how the interactions between telomeres and non-telomeric regions are established and regulated. We employ a telomere chromosome conformation capture (Telo-3C) approach to directly analyze telomere folding and its maintenance in S. cerevisiae. We identify the histone modifiers Sir2, Sin3 and Set2 as critical regulators for telomere folding, which suggests that a dis…

TelomeraseProtein Folding:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::DNA-Binding Proteins::Rad52 DNA Repair and Recombination Protein [Medical Subject Headings]:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Fungal Proteins::Saccharomyces cerevisiae Proteins [Medical Subject Headings]Gene ExpressionYeast and Fungal ModelsArtificial Gene Amplification and ExtensionQH426-470BiochemistryPolymerase Chain ReactionChromosome conformation captureHistonesCromatina0302 clinical medicineSirtuin 2Macromolecular Structure AnalysisSilent Information Regulator Proteins Saccharomyces cerevisiaeCellular Senescence:Organisms::Eukaryota::Fungi::Yeasts::Saccharomyces::Saccharomyces cerevisiae [Medical Subject Headings]0303 health sciencesChromosome BiologyEukaryota:Phenomena and Processes::Genetic Phenomena::Genetic Processes::DNA Replication [Medical Subject Headings]TelomereSubtelomere:Anatomy::Cells::Cellular Structures::Intracellular Space::Cell Nucleus::Cell Nucleus Structures::Intranuclear Space::Chromosomes::Chromosome Structures::Telomere [Medical Subject Headings]Chromatin3. Good healthChromatinCell biologyNucleic acidsTelomeres:Phenomena and Processes::Cell Physiological Phenomena::Cell Physiological Processes::Cell Cycle::Cell Division::Telomere Homeostasis [Medical Subject Headings]Experimental Organism SystemsDaño del ADNEpigeneticsResearch ArticleSenescenceDNA Replication:Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Hydrolases::Amidohydrolases::Histone Deacetylases [Medical Subject Headings]Chromosome Structure and FunctionProtein StructureSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeBiologyResearch and Analysis MethodsHistone DeacetylasesChromosomes03 medical and health sciencesSaccharomycesModel Organisms:Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Transferases::One-Carbon Group Transferases::Methyltransferases [Medical Subject Headings]:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Intracellular Signaling Peptides and Proteins::Sirtuins::Sirtuin 2 [Medical Subject Headings]:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Fungal Proteins::Saccharomyces cerevisiae Proteins::Silent Information Regulator Proteins Saccharomyces cerevisiae [Medical Subject Headings]DNA-binding proteinsGenetics:Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Recombinases::Rec A Recombinases::Rad51 Recombinase [Medical Subject Headings]Molecular Biology TechniquesMolecular Biology030304 developmental biologyCromosomasSenescencia celularOrganismsFungiBiology and Life SciencesProteinsTelomere HomeostasisCell BiologyDNAMethyltransferasesG2-M DNA damage checkpointProteína recombinante y reparadora de ADN Rad52YeastTelomereRad52 DNA Repair and Recombination ProteinRepressor ProteinsAnimal Studies:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Transcription Factors::Repressor Proteins [Medical Subject Headings]DNA damageRad51 RecombinaseHomologous recombination030217 neurology & neurosurgeryTelómeroDNA DamagePLoS Genetics
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Myriocin-induced adaptive laboratory evolution of an industrial strain of Saccharomyces cerevisiae reveals its potential to remodel lipid composition…

2020

The modification of lipid composition allows cells to adjust membrane biophysical properties in response to changes in environmental temperature. Here, we use adaptive laboratory evolution (ALE) in the presence of myriocin, a sphingolipid (SLs) biosynthesis inhibitor, to remodel the lipid profile of an industrial yeast strain (LH) of Saccharomyces cerevisiae. The approach enabled to obtain a heterogeneous population (LHev) of myriocin‐tolerant evolved clones characterized by its growth capacity at high temperature. Myriocin exposure also caused tolerance to soraphen A, an inhibitor of the acetyl‐CoA carboxylase Acc1, the rate‐limiting enzyme in fatty acid de novo production, supporting a ch…

ThermotoleranceBioquímicaSaccharomyces cerevisiae ProteinsSphingoid basesSaccharomyces cerevisiaePopulationPloidy levelMicrobiologiaBioengineeringSaccharomyces cerevisiaeApplied Microbiology and BiotechnologyBiochemistrySphingolipidFatty Acids Monounsaturated03 medical and health scienceschemistry.chemical_compoundMyriocinBaker’s yeasteducationFatty acid synthesisResearch Articles030304 developmental biologychemistry.chemical_classification0303 health scienceseducation.field_of_studybiologyStrain (chemistry)030306 microbiologyFatty acidLipid metabolismbiology.organism_classificationYeastHeat-stressPhospholipidTriacylgliceridechemistryBiochemistryLaboratoriesTP248.13-248.65BiotechnologyResearch Article
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Serine- and Threonine/Valine-Dependent Activation of PDK and Tor Orthologs Converge on Sch9 to Promote Aging

2014

Dietary restriction extends longevity in organisms ranging from bacteria to mice and protects primates from a variety of diseases, but the contribution of each dietary component to aging is poorly understood. Here we demonstrate that glucose and specific amino acids promote stress sensitization and aging through the differential activation of the Ras/cAMP/PKA, PKH1/2 and Tor/S6K pathways. Whereas glucose sensitized cells through a Ras-dependent mechanism, threonine and valine promoted cellular sensitization and aging primarily by activating the Tor/S6K pathway and serine promoted sensitization via PDK1 orthologs Pkh1/2. Serine, threonine and valine activated a signaling network in which Sch…

ThreonineCancer ResearchAgingSerineMice0302 clinical medicineSettore BIO/13 - Biologia ApplicataGene Expression Regulation FungalMolecular Cell BiologySerineSignaling in Cellular ProcessesThreonineGenetics (clinical)Cellular Stress Responses0303 health sciencesageing longevity Sch9 Tor Pkhs nutrients amino acidssurvival stress resistanceMechanisms of Signal TransductionValineCell biologyBiochemistryPhosphorylationSignal transductionResearch ArticleSignal TransductionSaccharomyces cerevisiae Proteinslcsh:QH426-470Adenylyl Cyclase Signaling PathwayLongevityP70-S6 Kinase 1Ras SignalingSaccharomyces cerevisiaeBiologyMicrobiologySignaling Pathways3-Phosphoinositide-Dependent Protein Kinases03 medical and health sciencesModel OrganismsStress PhysiologicalGeneticsAnimalsGene NetworksProtein kinase AMolecular BiologyTranscription factorBiologyEcology Evolution Behavior and Systematics030304 developmental biologySerine/threonine-specific protein kinase[SDV.GEN]Life Sciences [q-bio]/GeneticsCyclic AMP-Dependent Protein Kinaseslcsh:GeneticsGlucoseFoodTor SignalingProtein Kinases030217 neurology & neurosurgeryTranscription Factors
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Chromatin-dependent regulation of RNA polymerases II and III activity throughout the transcription cycle

2015

The particular behaviour of eukaryotic RNA polymerases along different gene regions and amongst distinct gene functional groups is not totally understood. To cast light onto the alternative active or backtracking states of RNA polymerase II, we have quantitatively mapped active RNA polymerases at a high resolution following a new biotin-based genomic run-on (BioGRO) technique. Compared with conventional profiling with chromatin immunoprecipitation, the analysis of the BioGRO profiles in Saccharomyces cerevisiae shows that RNA polymerase II has unique activity profiles at both gene ends, which are highly dependent on positioned nucleosomes. This is the first demonstration of the in vivo infl…

Transcription factoriesSaccharomyces cerevisiae ProteinsTranscription Elongation GeneticTranscription GeneticRNA polymerase II28Saccharomyces cerevisiaeBiology03 medical and health scienceschemistry.chemical_compoundTranscripció genèticaRNA polymeraseGeneticsRNA polymerase IRNA polymerase II holoenzyme9030304 developmental biologyGenetics0303 health sciencesGeneral transcription factorGene regulation Chromatin and Epigenetics030302 biochemistry & molecular biologyRNA Polymerase IIIGenomicsNucleosomesCell biologychemistryTranscription Termination Geneticbiology.proteinRNARNA Polymerase IIGenome FungalTranscription factor II DSmall nuclear RNA
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A complete set of nascent transcription rates for yeast genes

2010

The amount of mRNA in a cell is the result of two opposite reactions: transcription and mRNA degradation. These reactions are governed by kinetics laws, and the most regulated step for many genes is the transcription rate. The transcription rate, which is assumed to be exercised mainly at the RNA polymerase recruitment level, can be calculated using the RNA polymerase densities determined either by run-on or immunoprecipitation using specific antibodies. The yeast Saccharomyces cerevisiae is the ideal model organism to generate a complete set of nascent transcription rates that will prove useful for many gene regulation studies. By combining genomic data from both the GRO (Genomic Run-on) a…

Transcription factoriesSaccharomyces cerevisiae ProteinsTranscription GeneticRNA StabilityGenes FungalDNA transcriptionlcsh:MedicineYeast and Fungal ModelsRNA polymerase IISaccharomyces cerevisiaeBiologyBiochemistryGenètica molecularchemistry.chemical_compoundSaccharomycesModel OrganismsMolecular cell biologyTranscripció genèticaGene Expression Regulation FungalRNA polymeraseGeneticsRNA MessengerRNA synthesislcsh:ScienceBiologyRNA polymerase II holoenzymeGeneticsMultidisciplinaryGeneral transcription factorGene Expression Profilinglcsh:RPromoterGenomicsChromatinFunctional GenomicsNucleic acidsGenòmicaRNA processingchemistrybiology.proteinRNAlcsh:QRNA Polymerase IIGene expressionTranscription factor II DTranscription factor II BResearch Article
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Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery

2004

12 páginas, 7 figuras, 1 tabla. Material suplementario en: https://doi.org/10.1016/S0092-8674(03)01025-0. The SUS1 sequences have been deposited in GenBank with the accession number AY278445.

Transcriptional ActivationNucleocytoplasmic Transport ProteinsDNA ComplementarySaccharomyces cerevisiae ProteinsMolecular Sequence DataActive Transport Cell NucleusPorinsRNA polymerase IIBiologyGeneral Biochemistry Genetics and Molecular BiologyFungal ProteinsTranscription (biology)AcetyltransferasesGene Expression Regulation FungalYeastsGene expressionGenes RegulatorTranscriptional regulationAmino Acid SequenceRNA MessengerNuclear proteinPromoter Regions GeneticHistone AcetyltransferasesRegulation of gene expressionCell NucleusBase SequenceBiochemistry Genetics and Molecular Biology(all)Nuclear ProteinsRNA-Binding ProteinsMolecular biologyCell biologySAGA complexRibonucleoproteinsbiology.proteinNuclear PoreGenes LethalChromatin immunoprecipitation
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The yeast Aft1 transcription factor activates ribonucleotide reductase catalytic subunit RNR1 in response to iron deficiency

2020

Eukaryotic ribonucleotide reductases are iron-dependent enzymes that catalyze the rate-limiting step in the de novo synthesis of deoxyribonucleotides. Multiple mechanisms regulate the activity of ribonucleotide reductases in response to genotoxic stresses and iron deficiency. Upon iron starvation, the Saccharomyces cerevisiae Aft1 transcription factor specifically binds to iron-responsive cis elements within the promoter of a group of genes, known as the iron regulon, activating their transcription. Members of the iron regulon participate in iron acquisition, mobilization and recycling, and trigger a genome-wide metabolic remodeling of iron-dependent pathways. Here, we describe a mechanism …

Transcriptional ActivationRibonucleotideSaccharomyces cerevisiae ProteinsProtein subunitIronSaccharomyces cerevisiaeDeoxyribonucleotidesBiophysicsSaccharomyces cerevisiaeResponse ElementsBiochemistry03 medical and health sciencesStructural BiologyTranscription (biology)Gene Expression Regulation FungalRibonucleotide ReductasesGeneticsMolecular BiologyTranscription factorRibonucleotide reductase030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyChemistryIron deficiency030302 biochemistry & molecular biologyHigh Mobility Group ProteinsIron Deficienciesbiology.organism_classificationCell biologyDNA-Binding ProteinsRibonucleotide reductaseRegulonEnzymeYeast/TranscriptionProtein BindingTranscription Factors
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Yeast karyopherin Kap95 is required for cell cycle progression at Start

2010

Abstract Background The control of the subcellular localization of cell cycle regulators has emerged as a crucial mechanism in cell division regulation. The active transport of proteins between the nucleus and the cytoplasm is mediated by the transport receptors of the β-karyopherin family. In this work we characterized the terminal phenotype of a mutant strain in β-karyopherin Kap95, a component of the classical nuclear import pathway. Results When KAP95 was inactivated, most cells arrested at the G2/M phase of the cell cycle, which is in agreement with the results observed in mutants in the other components of this pathway. However, a number of cells accumulate at G1, suggesting a novel r…

Transcriptional ActivationSaccharomyces cerevisiae ProteinsNuclear Localization SignalsActive Transport Cell NucleusSaccharomyces cerevisiaeImportinBiologylcsh:QH573-671Transcription factorCells CulturedKaryopherinCell Nucleuschemistry.chemical_classificationlcsh:CytologyCell CycleCell BiologyCell cyclebeta KaryopherinsSubcellular localizationCell biologyDNA-Binding ProteinschemistryCytoplasmMutationTranscription Initiation SiteNuclear transportNuclear localization sequenceProtein BindingTranscription FactorsResearch ArticleBMC Cell Biology
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Fertility and Polarized Cell Growth Depends on eIF5A for Translation of Polyproline-Rich Formins in Saccharomyces cerevisiae

2014

eIF5A is an essential and evolutionary conserved translation elongation factor, which has recently been proposed to be required for the translation of proteins with consecutive prolines. The binding of eIF5A to ribosomes occurs upon its activation by hypusination, a modification that requires spermidine, an essential factor for mammalian fertility that also promotes yeast mating. We show that in response to pheromone, hypusinated eIF5A is required for shmoo formation, localization of polarisome components, induction of cell fusion proteins, and actin assembly in yeast. We also show that eIF5A is required for the translation of Bni1, a proline-rich formin involved in polarized growth during …

TranslationSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaePeptide Chain Elongation TranslationalForminsRNA-binding proteinSaccharomyces cerevisiaeInvestigationsPeptide Initiation FactorsMorphogenesisGeneticsQc-SNARE ProteinsPolyproline helixPolarisomeGeneticsMatingbiologyMicrofilament ProteinsMembrane ProteinsRNA-Binding ProteinsTranslation (biology)Polarized growthbiology.organism_classificationActinsProtein Structure TertiaryCell biologyCytoskeletal ProteinsMating of yeastForminsMutationbiology.proteinEIF5APeptidesRibosomesEIF5A
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