Search results for "VISIA"

showing 10 items of 764 documents

The YJL185C, YLR376C and YJR129C genes of Saccharomyces cerevisiae are probably involved in regulation of the glyoxylate cycle

2006

The ER24 aci (acidification) mutant of Saccharomyces cerevisiae excreting protons in the absence of glucose was transformed with a multicopy yeast DNA plasmid library. Three different DNA fragments restored the wild-type phenotype termed Aci- because it does not acidify the complete glucose medium under the tested conditions. Molecular dissection of the transforming DNA fragments identified two multicopy suppressor genes YJL185C, YJR129C and one allelic YLR376C. Disruption of either of the three genes in wild-type yeast strain resulted in acidification of the medium (Aci+ phenotype) similarly to the original ER24 mutant. These data indicate the contribution of the ER24 gene product Ylr376Cp…

Saccharomyces cerevisiae ProteinsMutantSaccharomyces cerevisiaeGenes FungalGlyoxylate cycleAutophagy-Related ProteinsGlyoxylatesMethyltransferasesSaccharomyces cerevisiaeBiologyHydrogen-Ion Concentrationbiology.organism_classificationGeneral Biochemistry Genetics and Molecular BiologyYeastCulture MediaGene productchemistry.chemical_compoundPlasmidchemistryBiochemistryGenes SuppressorGeneDNAMetabolic Networks and Pathways
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Molecular structure of the cell wall receptor for killer toxin KT28 in Saccharomyces cerevisiae

1988

The adsorption of the yeast killer toxin KT28 to susceptible cells of Saccharomyces cerevisiae was prevented by concanavalin A, which blocks the mannoprotein receptor. Certain mannoprotein mutants of S. cerevisiae that lack definite structures in the mannan of their cell walls were found to be resistant to KT28, whereas the wild-type yeast from which the mutants were derived was susceptible. Isolated mannoprotein from a resistant mutant was unable to adsorb killer toxin. By comparing the resistances of different mannoprotein mutants, information about the molecular structure of the receptor was obtained. At least two mannose residues have to be present in the side chains of the outer chain …

Saccharomyces cerevisiae ProteinsMutantSaccharomyces cerevisiaeMannoseReceptors Cell Surfacechemical and pharmacologic phenomenaSaccharomyces cerevisiaeSpheroplastsMicrobiologyFungal Proteinschemistry.chemical_compoundCell WallConcanavalin AReceptorMolecular BiologyGlycoproteinsMannanMembrane GlycoproteinsbiologyMycotoxinsSpheroplastbiology.organism_classificationKiller Factors YeastYeastcarbohydrates (lipids)BiochemistrychemistryConcanavalin AMutationbiology.proteinAdsorptionResearch ArticleJournal of Bacteriology
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Effects of yeast proteolytic activity on Oenococcus oeni and malolactic fermentation

2006

International audience; Alcoholic fermentation of synthetic must was performed using either Saccharomyces cerevisiae or a mutant Delta pep4, which is deleted for the proteinase A gene. Fermentation with the mutant Delta pep4 resulted in 61% lower levels of free amino acids, and in 62% lower peptide concentrations at the end of alcoholic fermentation than in the control. Qualitative differences in amino acid composition were observed. Changes observed in amino acids in peptides were mainly quantitative. After alcoholic fermentation each medium was inoculated with Oenococcus oeni. Malolactic fermentation in the medium with the Delta pep4 strain took 10 days longer than the control. This diffe…

Saccharomyces cerevisiae ProteinsNitrogenMalatesWineSaccharomyces cerevisiaeEthanol fermentationMicrobiology03 medical and health sciencesMalate DehydrogenaseProteinase APEP4EndopeptidasesGeneticsMalolactic fermentationLactic acid bacteriaNitrogen metabolismAmino AcidsMolecular Biology030304 developmental biologyOenococcus oenichemistry.chemical_classification0303 health sciencesbiology030306 microbiologyProteolytic enzymesfood and beveragesFree amino nitrogenbiology.organism_classificationYeastYeastAmino acidGram-Positive Cocci[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologychemistryBiochemistryFermentationPeptideFermentation
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Molecular response of Saccharomyces cerevisiae wine and laboratory strains to high sugar stress conditions.

2010

One of the stress conditions that can affect Saccharomyces cerevisiae cells during their growth is osmotic stress. Under particular environments (for instance, during the production of alcoholic beverages) yeasts have to cope with osmotic stress caused by high sugar concentrations. Although the molecular changes and pathways involved in the response to saline or sorbitol stress are widely understood, less is known about how cells respond to high sugar concentrations. In this work we present a comprehensive study of the response to this form of stress which indicates important transcriptomic changes, especially in terms of the genes involved in both stress response and respiration, and the i…

Saccharomyces cerevisiae ProteinsOsmotic shockProteomeMutantSaccharomyces cerevisiaeWineSaccharomyces cerevisiaeBiologyMicrobiologychemistry.chemical_compoundStress PhysiologicalGene Expression Regulation FungalGene expressionPhosphorylationOligonucleotide Array Sequence AnalysisGene Expression ProfilingRNA FungalGeneral Medicinebiology.organism_classificationYeastGlucosechemistryBiochemistryMolecular ResponseProteomeMutationSorbitolMitogen-Activated Protein KinasesFood ScienceInternational journal of food microbiology
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Recruitment of Xrn1 to stress-induced genes allows efficient transcription by controlling RNA polymerase II backtracking

2020

A new paradigm has emerged proposing that the crosstalk between nuclear transcription and cytoplasmic mRNA stability keeps robust mRNA levels in cells under steady-state conditions. A key piece in this crosstalk is the highly conserved 5′–3′ RNA exonuclease Xrn1, which degrades most cytoplasmic mRNAs but also associates with nuclear chromatin to activate transcription by not well-understood mechanisms. Here, we investigated the role of Xrn1 in the transcriptional response of Saccharomyces cerevisiae cells to osmotic stress. We show that a lack of Xrn1 results in much lower transcriptional induction of the upregulated genes but in similar high levels of their transcripts because of parallel …

Saccharomyces cerevisiae ProteinsOsmotic shockTranscription GeneticRNA StabilityRNA polymerase IISaccharomyces cerevisiaeBiology03 medical and health sciences0302 clinical medicineTranscription (biology)Gene Expression Regulation FungalRNA MessengerMolecular BiologyGene030304 developmental biology0303 health sciencesMessenger RNABacktrackingRNA FungalCell BiologyCell biologyCrosstalk (biology)Cytoplasm030220 oncology & carcinogenesisExoribonucleasesbiology.proteinRNA Polymerase IIResearch Paper
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Cooperation of Two mRNA-Binding Proteins Drives Metabolic Adaptation to Iron Deficiency

2008

Summary Iron (Fe) is an essential cofactor for a wide range of cellular processes. We have previously demonstrated in yeast that Cth2 is expressed during Fe deficiency and promotes degradation of a battery of mRNAs leading to reprogramming of Fe-dependent metabolism and Fe storage. We report here that the Cth2-homologous protein Cth1 is transiently expressed during Fe deprivation and participates in the response to Fe deficiency through the degradation of mRNAs primarily involved in mitochondrially localized activities including respiration and amino acid biosynthesis. In parallel, wild-type cells, but not cth1 Δ cth2 Δ cells, accumulate mRNAs encoding proteins that function in glucose impo…

Saccharomyces cerevisiae ProteinsPhysiologySaccharomyces cerevisiaeHUMDISEASERNA-binding proteinSaccharomyces cerevisiaeProtein Serine-Threonine KinasesDNA-binding proteinArticlechemistry.chemical_compoundTristetraprolinGlucose importRNA MessengerPhosphorylationProtein kinase AMolecular BiologybiologyGlycogenRNA-Binding ProteinsIron DeficienciesCell BiologyMetabolismbiology.organism_classificationAdaptation PhysiologicalDNA-Binding ProteinsMetabolismBiochemistrychemistryPhosphorylationTranscription FactorsCell Metabolism
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Protein Interactions within the Set1 Complex and Their Roles in the Regulation of Histone 3 Lysine 4 Methylation

2006

Set1 is the catalytic subunit and the central component of the evolutionarily conserved Set1 complex (Set1C) that methylates histone 3 lysine 4 (H3K4). Here we have determined protein/protein interactions within the complex and related the substructure to function. The loss of individual Set1C subunits differentially affects Set1 stability, complex integrity, global H3K4 methylation, and distribution of H3K4 methylation along active genes. The complex requires Set1, Swd1, and Swd3 for integrity, and Set1 amount is greatly reduced in the absence of the Swd1-Swd3 heterodimer. Bre2 and Sdc1 also form a heteromeric subunit, which requires the SET domain for interaction with the complex, and Sdc…

Saccharomyces cerevisiae ProteinsProtein subunitLysineRNA polymerase IISaccharomyces cerevisiaeMethylationenvironment and public healthBiochemistryProtein–protein interactionHistonesSerineGene Expression Regulation FungalCoding regionMolecular BiologybiologyLysineHistone-Lysine N-MethyltransferaseCell BiologyMethylationDNA-Binding ProteinsProtein SubunitsHistoneBiochemistrybiology.proteinProtein BindingTranscription FactorsJournal of Biological Chemistry
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Transcriptomic and Proteomic Approach for Understanding the Molecular Basis of Adaptation of Saccharomyces cerevisiae to Wine Fermentation

2006

ABSTRACT Throughout alcoholic fermentation, Saccharomyces cerevisiae cells have to cope with several stress conditions that could affect their growth and viability. In addition, the metabolic activity of yeast cells during this process leads to the production of secondary compounds that contribute to the organoleptic properties of the resulting wine. Commercial strains have been selected during the last decades for inoculation into the must to carry out the alcoholic fermentation on the basis of physiological traits, but little is known about the molecular basis of the fermentative behavior of these strains. In this work, we present the first transcriptomic and proteomic comparison between …

Saccharomyces cerevisiae ProteinsProteomeTranscription GeneticSaccharomyces cerevisiaeSulfur metabolismWineSaccharomyces cerevisiaeEthanol fermentationBiologyApplied Microbiology and BiotechnologyGene Expression Regulation FungalHeat shock proteinFermentation in winemakingWineEcologyGene Expression ProfilingPhysiology and Biotechnologybiology.organism_classificationAdaptation PhysiologicalYeastBiochemistryFermentationFermentationHeat-Shock ResponseFood ScienceBiotechnologyApplied and Environmental Microbiology
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Bromodomain factor 1 (Bdf1) protein interacts with histones

2001

AbstractUsing a yeast two-hybrid assay we detected an interaction between the N-terminal region of histone H4 (amino acids 1–59) and a fragment of the bromodomain factor 1 protein (Bdf1p) (amino acids 304–571) that includes one of the two bromodomains of this protein. No interaction was observed using fragments of histone H4 sequence smaller than the first 59 amino acids. Recombinant Bdf1p (rBdf1p) demonstrates binding affinity for histones H4 and H3 but not H2A and H2B in vitro. Moreover, rBdf1p is able to bind histones H3 and H4 having different degrees of acetylation. Finally, we have not detected histone acetyltransferase activity associated with Bdf1p.

Saccharomyces cerevisiae ProteinsRecombinant Fusion ProteinsBiophysicsBromodomainTwo-hybridBiochemistryFungal ProteinsHistonesHistone H4SaccharomycesAcetyltransferasesGenes ReporterStructural BiologyTwo-Hybrid System TechniquesHistone methylationHistone H2AGeneticsHistone acetyltransferase activityHistone octamerMolecular BiologyHistone AcetyltransferasesBromodomain factor 1 proteinbiologyChemistryCell BiologyHistone acetyltransferasePeptide FragmentsChromatinBromodomainHistoneBiochemistryPCAFbiology.proteinHistone acetyltransferaseProtein BindingTranscription FactorsFEBS Letters
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The C-terminal region of the Hot1 transcription factor binds GGGACAAA-related sequences in the promoter of its target genes

2015

Response to hyperosmotic stress in the yeast Saccharomyces cerevisiae involves the participation of the general stress response mediated by Msn2/4 transcription factors and the HOG pathway. One of the transcription factors activated through this pathway is Hot1, which contributes to the control of the expression of several genes involved in glycerol synthesis and flux, or in other functions related to adaptation to adverse conditions. This work provides new data about the interaction mechanism of this transcription factor with DNA. By means of one-hybrid and electrophoretic mobility assays, we demonstrate that the C-terminal region, which corresponds to amino acids 610-719, is the DNA-bindi…

Saccharomyces cerevisiae ProteinsRecombinant Fusion ProteinsGenes FungalMolecular Sequence DataResponse elementBiophysicsE-boxSequence alignmentSaccharomyces cerevisiaeBiologyBiochemistryConserved sequenceOsmoregulationStructural BiologyGene Expression Regulation FungalGeneticsComputer SimulationAmino Acid SequenceDNA FungalPromoter Regions GeneticMolecular BiologyTranscription factorConserved SequenceSequence DeletionCis-regulatory moduleGeneticsBinding SitesBase SequenceSequence Homology Amino AcidMembrane Transport ProteinsPromoterDNA-binding domainProtein Structure TertiaryMutationSequence AlignmentProtein BindingTranscription FactorsBiochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms
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