Search results for "SIAE"

showing 10 items of 787 documents

Limitēta skābekļa apstākļos kultivēta rauga anhidrobioze un tās biotehnoloģiskie pielietojumi

2018

Promocijas darba gaitā izvērtētas iespējas uzlabot raugu Saccharomyces cerevisiae kultivētu limitēta skābekļa apstākļos izturību dehidratācijas-rehidratācijas procesā. Izpētīta dažādu vielu - antioksidantu, cukuru, sāls, poliolu - iespējamā ietekme uz šūnu rezistences palielināšanu. Tāpat parādīta iespēja izmantot celulozi saturošu substrātu pēc furfurola izdalīšanas etanola sintēzei. Pētījumos noskaidroti apstākļi enzimātiskās hidrolīzes procesam un papildus priekšapstrādes izmantošanas efektivitāte glikozes iznākuma uzlabošanai, kā arī iegūtā hidrolizāta un dehidratēto raugu izmantošanas iespējas. Promocijas darbā novērotās likumsakarības raugu šūnu atbildes reakcijās uz inkubācijas priek…

MikrobioloģijaanhidrobiozebioetanolsSaccharomyces cerevisiaeBioloģijaMicrobiology
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Mitochondrial inheritance and fermentative : oxidative balance in hybrids between Saccharomyces cerevisiae and Saccharomyces uvarum.

2008

Breeding between Saccharomyces species is a useful tool for obtaining improved wine yeast strains, combining fermentative features of parental species. In this work, 25 artificial Saccharomyces cerevisiae × Saccharomyces uvarum hybrids were constructed by spore conjugation. A multi-locus PCR‐restriction fragment length polymorphism (PCR‐RFLP) analysis, targeting six nuclear gene markers and the ribosomal region including the 5.8S rRNA gene and the two internal transcribed spacers, showed that the hybrid genome is the result of two chromosome sets, one coming from S. cerevisiae and the other from S. uvarum. Mitochondrial DNA (mtDNA) typing showed uniparental inheritance in all hybrids. Furth…

Mitochondrial DNANuclear geneSaccharomyces cerevisiaeUniparental inheritanceBioengineeringSaccharomyces cerevisiaeBiologyApplied Microbiology and BiotechnologyBiochemistryGenomeDNA MitochondrialDNA RibosomalPolymerase Chain ReactionSaccharomyces cerevisiae; Saccharomyces uvarum; yeast hybrid; gene expression; mitochondrial DNAGeneticsMycological Typing TechniquesGeneHexose transportCrosses GeneticGeneticsRibosomal RNAbiology.organism_classificationRNA Ribosomal 5.8SGenes MitochondrialFermentationHybridization GeneticBiotechnologyYeast (Chichester, England)
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Mitochondria inheritance is a key factor for tolerance to dehydration in wine yeast production

2015

UNLABELLED Mitochondria are the cell's powerhouse when organisms are grown in the presence of oxygen. They are also the source of reactive oxygen species that cause damage to the biochemical components of the cell and lead to cellular ageing and death. Under winemaking conditions, Saccharomyces yeasts exclusively have a fermentative metabolism due to the high sugar content of grape must. However, their production as an active dry yeast (ADY) form required aerobic propagation and a dehydration process. In these industrial steps, oxidative stress is particularly harmful for the cell. In this work, we analysed the impact of the mitochondrial genome on oxidative stress response, longevity and d…

Mitochondrial DNASaccharomyces cerevisiaeSaccharomyces cerevisiaeMitochondrionyeastmedicine.disease_causeApplied Microbiology and BiotechnologySaccharomyces03 medical and health sciences[SDV.IDA]Life Sciences [q-bio]/Food engineeringmedicineoxidative stressVitis[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringDesiccationwine030304 developmental biology2. Zero hunger0303 health sciencesMitochondrial DNA inheritancebiology030306 microbiologydehydrationbiology.organism_classificationYeastmitochondriaYeast in winemakingBiochemistryFermentationReactive Oxygen SpeciesOxidative stresslifespan
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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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Mitotic Recombination and Genetic Changes in Saccharomyces cerevisiae during Wine Fermentation

2000

Natural strains of Saccharomyces cerevisiae are prototrophic homothallic yeasts that sporulate poorly, are often heterozygous, and may be aneuploid. This genomic constitution may confer selective advantages in some environments. Different mechanisms of recombination, such as meiosis or mitotic rearrangement of chromosomes, have been proposed for wine strains. We studied the stability of the URA3 locus of a URA3/ura3 wine yeast in consecutive grape must fermentations. ura3/ura3 homozygotes were detected at a rate of 1 x 10(-5) to 3 x 10(-5) per generation, and mitotic rearrangements for chromosomes VIII and XII appeared after 30 mitotic divisions. We used the karyotype as a meiotic marker an…

Mitotic crossoverSaccharomyces cerevisiaeMitosisGenetics and Molecular BiologyWineSaccharomyces cerevisiaeApplied Microbiology and BiotechnologyGenetic recombinationFungal ProteinsMeiosisFermentacióDNA FungalMitosisGeneticsFermentation in winemakingRecombination GeneticEcologybiologyHomozygotefood and beveragesvinificationSpores Fungalbiology.organism_classificationElectrophoresis Gel Pulsed-FieldYeast in winemakingMeiosiswine fermentationKaryotypingFermentationMitotic recombinationChromosomes FungalHomologous recombinationFood ScienceBiotechnology
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Comparison of Protective Effects against Reactive Oxygen Species of Mononuclear and Dinuclear Cu(II) Complexes with N-Substituted Benzothiazolesulfon…

2005

Copper(II) complexes of N-benzothiazolesulfonamides (HL1=N-2-(4-methylphenylsulfamoyl)-6-nitro-benzothiazole, HL2=N-2-(phenylsulfamoyl)-6-chloro-benzothiazole, and HL3=N-2-(4-methylphenylsulfamoyl)-6-chloro-benzothiazole) with ammonia have been synthesized and characterized. The crystal structures of the [Cu(L1)2(NH3)2].2MeOH, [Cu(L2)2(NH3)2], and [Cu(L3)2(NH3)2] compounds have been determined. Compounds and present a distorted square planar geometry. In both compounds the metal ion is coordinated by two benzothiazole N atoms from two sulfonamidate anions and two NH3 molecules. Complex is distorted square-pyramidal. The Cu(II) ion is linked to the benzothiazole N and sulfonamidate O atoms o…

Models MolecularFree RadicalsStereochemistrychemistry.chemical_elementSaccharomyces cerevisiaeCrystal structureIn Vitro TechniquesCrystallography X-RayMedicinal chemistryIonInorganic ChemistryMetalSuperoxide dismutaseStructure-Activity RelationshipAmmoniachemistry.chemical_compoundOrganometallic CompoundsMoleculeBenzothiazolesPhysical and Theoretical ChemistrySulfonamidesMolecular StructurebiologySuperoxide DismutaseCopperchemistryBenzothiazolevisual_artvisual_art.visual_art_mediumbiology.proteinCrystallizationReactive Oxygen SpeciesCopperInorganic Chemistry
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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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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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