Search results for "Saccharomyce"

showing 10 items of 875 documents

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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Homology modeling using simulated annealing of restrained molecular dynamics and conformational search calculations with CONGEN: application in predi…

1997

We have developed an automatic approach for homology modeling using restrained molecular dynamics and simulated annealing procedures, together with conformational search algorithms available in the molecular mechanics program CONGEN (Bruccoleri RE, Karplus M, 1987, Biopolymers 26:137-168). The accuracy of the method is validated by "predicting" structures of two homeodomain proteins with known three-dimensional structures, and then applied to predict the three-dimensional structure of the homeodomain of the murine Msx-1 transcription factor. Regions of the unknown protein structure that are highly homologous to the known template structure are constrained by "homology distance constraints,"…

Models MolecularSaccharomyces cerevisiae ProteinsProtein ConformationMSX1 Transcription FactorMolecular Sequence DataSaccharomyces cerevisiaeBiologyProtein EngineeringBiochemistryProtein Structure SecondaryMolecular dynamicsMiceProtein structureAnimalsComputer SimulationHomology modelingAmino Acid SequenceMolecular BiologyHomeodomain ProteinsMSX1 Transcription FactorSequence Homology Amino AcidNuclear ProteinsProtein engineeringProtein superfamilyengrailedRepressor ProteinsCrystallographyAntennapedia Homeodomain ProteinThreading (protein sequence)AlgorithmsInformation SystemsTranscription FactorsResearch ArticleProtein science : a publication of the Protein Society
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Characterization of aCandida albicansgene encoding a putative transcriptional factor required for cell wall integrity

2003

After screening a Candida albicans genome database the product of an open reading frame (ORF) (CA2880) with 49% homology to the product of Saccharomyces cerevisiae YPL133c, a putative transcriptional factor, was identified. The disruption of the C. albicans gene leads to a major sensitivity to calcofluor white and Congo red, a minor sensitivity to sodium dodecyl sulfate, a major resistance to zymolyase, and an alteration of the chemical composition of the cell wall. For these reasons we called it CaCWT1 (for C. albicans cell wall transcription factor). CaCwt1p contains a putative Zn(II) Cys(6) DNA binding domain characteristic of some transcriptional factors and a PAS domain. The CaCWT1 gen…

Models MolecularTranscription GeneticGenes FungalMolecular Sequence DataSaccharomyces cerevisiaeSequence HomologyMicrobiologyFungal ProteinsCell WallPAS domainGene Expression Regulation FungalCandida albicansGenes RegulatorGeneticsAmino Acid SequenceColoring AgentsCandida albicansMolecular BiologyGeneTranscription factorbiologyReverse Transcriptase Polymerase Chain ReactionGlucan Endo-13-beta-D-GlucosidaseComputational BiologySodium Dodecyl SulfateDNA-binding domainbiology.organism_classificationMolecular biologyCorpus albicansDNA-Binding ProteinsMutagenesis InsertionalOpen reading frameGenome FungalGene DeletionTranscription FactorsFEMS Microbiology Letters
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Effect of tin and lead chlorotriphenyl analogues on selected living cells.

2010

Three kinds of living cells, human embryonic kidney cells, Saccharomyces cerevisiae, and Escherichia coli, were tested for their sensitivity to chlorotriphenyltin and chlorotriphenyllead. The tin compound proved definitely more toxic than the lead derivative, particularly in the case of the human embryonic kidney cells devoid of any protective cell wall. Electron paramagnetic resonance (EPR) comparative studies carried out by using a natural model liposome system (egg yolk lecithin) confirmed considerable changes within the lipid bilayer upon doping by the aforementioned additives, which may be crucial to the mechanism of the observed cell cleavage. The individual dopants revealed diverse i…

Models Molecularfood.ingredientCell SurvivalHealth Toxicology and MutagenesisCellMolecular Conformationchemistry.chemical_elementSaccharomyces cerevisiaeToxicologyCleavage (embryo)BiochemistryLecithinCell wallfoodLecithinsmedicineEscherichia coliOrganometallic CompoundsOrganotin CompoundsHumansChlorotriphenyltinLipid bilayerMolecular BiologyLiposomeElectron Spin Resonance SpectroscopyGeneral MedicineYeastChlorotriphenylleadElectron Paramagnetic Resonancemedicine.anatomical_structureMembraneHEK293 CellsBiochemistrychemistryLeadHuman Embryonic Kidney CellsLiposomesMolecular MedicineTinJournal of biochemical and molecular toxicology
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Chimeric Genomes of Natural Hybrids of Saccharomyces cerevisiae and Saccharomyces kudriavzevii

2009

11 pages, 6 figures.-- PMID: 19251887 [PubMed].-- Printed version published Apr 2009.

Molecular Sequence DataSaccharomyces cerevisiaeNatural hybridsWineSaccharomyces cerevisiaeBiologyApplied Microbiology and BiotechnologySaccharomycesGenomeGenètica molecularSaccharomycesMeiosisaCGHEvolutionary and Genomic MicrobiologyDNA FungalGeneGene RearrangementRecombination GeneticGeneticsComparative Genomic HybridizationEcologyChromosomeqRT-PCRSequence Analysis DNAbiology.organism_classificationAneuploidyDNA FingerprintingChromosome DeletionGenome FungalRestriction fragment length polymorphismSaccharomyces kudriavzeviiRecombination pointsPolymorphism Restriction Fragment LengthSaccharomyces kudriavzeviiFood ScienceBiotechnologyGenome hybridization
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Polypeptide composition of invertase-containing vesicles of Saccharomyces cerevisiae

1990

Vesicles containing invertase activity were obtained from protoplast homogenates of Saccharomyces cerevisiae by differential centrifugation followed by gel chromatography. These vesicles were similar in size and shape to yeast coated vesicles, and appear to have a complex polypeptide composition. Most of these polypeptides were seemingly bound to the surface of the vesicular structures, being released by treatment with alkali. A protein with an electrophoretic mobility similar to that of yeast clathrin (molecular mass of 185 kDa) co-purified with vesicles containing invertase activity, and exhibited cross-reactivity with anti-mammalian (pig) clathrin antibodies.

Molecular massbiologyVesicleSaccharomyces cerevisiaeCoated vesiclePlant ScienceProtoplastbiology.organism_classificationClathrinYeastInvertaseBiochemistryGeneticsbiology.proteinEcology Evolution Behavior and SystematicsBiotechnologyMycological Research
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A feedback mechanism controls rDNA copy number evolution in yeast independently of natural selection.

2022

Ribosomal DNA (rDNA) is the genetic loci that encodes rRNA in eukaryotes. It is typically arranged as tandem repeats that vary in copy number within the same species. We have recently shown that rDNA repeats copy number in the yeast Saccharomyces cerevisiae is controlled by cell volume via a feedback circuit that senses cell volume by means of the concentration of the free upstream activator factor (UAF). The UAF strongly binds the rDNA gene promoter, but is also able to repress SIR2 deacetylase gene transcription that, in turn, represses rDNA amplification. In this way, the cells with a smaller DNA copy number than what is optimal evolve to increase that copy number until they reach a numb…

MultidisciplinarySaccharomyces cerevisiae ProteinsDNA Copy Number VariationsSelecció naturalSaccharomyces cerevisiaeSelection GeneticCicle cel·lularDNA RibosomalEvolució (Biologia)FeedbackTranscription FactorsPloS one
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RNA-controlled nucleocytoplasmic shuttling of mRNA decay factors regulates mRNA synthesis and a novel mRNA decay pathway.

2021

AbstractmRNA level is controlled by factors that mediate both mRNA synthesis and decay, including the 5’ to 3’ exonuclease Xrn1. Here we show that nucleocytoplasmic shuttling of several yeast mRNA decay factors plays a key role in determining both mRNA synthesis and decay. Shuttling is regulated by RNA-controlled binding of the karyopherin Kap120 to two nuclear localization sequences (NLSs) in Xrn1, location of one of which is conserved from yeast to human. The decaying RNA binds and masks NLS1, establishing a link between mRNA decay and Xrn1 shuttling. Preventing Xrn1 import, either by deleting KAP120 or mutating the two Xrn1 NLSs, compromises transcription and, unexpectedly, also cytoplas…

MultidisciplinaryTranscription GeneticRNA StabilityGeneral Physics and AstronomyHumansRNAGeneral ChemistrySaccharomyces cerevisiaeRNA MessengerGeneral Biochemistry Genetics and Molecular BiologyGenètica molecularNature communications
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