Search results for "VISIA"

showing 10 items of 764 documents

Site specificity of pea histone acetyltransferase B in vitro.

1993

Histone acetyltransferase B from pea embryonic axes has been purified approximately 300-fold by a combination of chromatographic procedures, including affinity chromatography on histone-agarose. The enzyme preparation has been used for the in vitro transfer of acetyl groups from [1-14C]acetyl-CoA to non-acetylated pea histone H4. Up to three acetyl groups can be introduced into the histone. The resulting mono-, di-, and triacetylated H4 isoforms were separated and sequenced to determine the acetylated sites. Only sites 5, 12, and 16 were used by histone acetyltransferase B, but no clear preference among them was observed. The absence of modification of other potentially acetylatable sites i…

Saccharomyces cerevisiae ProteinsLysineMolecular Sequence DataBiochemistryChromatography AffinitySubstrate SpecificityHistone H4HistonesAffinity chromatographyAcetyltransferasesHistone octamerAmino Acid SequenceMolecular BiologyHistone AcetyltransferasesPlants MedicinalbiologyAcetylationFabaceaeCell BiologyHistone acetyltransferaseMolecular biologyIsoenzymesHistoneBiochemistryAcetylationHistone methyltransferasebiology.proteinElectrophoresis Polyacrylamide GelThe Journal of biological chemistry
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Characterization of the Viable but Nonculturable (VBNC) State in Saccharomyces cerevisiae

2013

The Viable But Non Culturable (VBNC) state has been thoroughly studied in bacteria. In contrast, it has received much less attention in other microorganisms. However, it has been suggested that various yeast species occurring in wine may enter in VBNC following sulfite stress.In order to provide conclusive evidences for the existence of a VBNC state in yeast, the ability of Saccharomyces cerevisiae to enter into a VBNC state by applying sulfite stress was investigated. Viable populations were monitored by flow cytometry while culturable populations were followed by plating on culture medium. Twenty-four hours after the application of the stress, the comparison between the culturable populat…

Saccharomyces cerevisiae ProteinsMicroorganismAnion Transport ProteinsSaccharomyces cerevisiaePopulationMutantlcsh:MedicineSaccharomyces cerevisiaeViable but nonculturableMicrobiologySulfiteslcsh:Scienceeducationeducation.field_of_studyMultidisciplinarybiologyCell Cyclelcsh:RHydrogen-Ion Concentrationbiology.organism_classificationYeastCulture MediaMolecular mechanismlcsh:QBacteriaResearch ArticlePLoS ONE
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Functional Connection Between the Clb5 Cyclin, the Protein Kinase C Pathway and the Swi4 Transcription Factor in Saccharomyces cerevisiae

2005

Abstract The rsf12 mutation was isolated in a synthetic lethal screen for genes functionally interacting with Swi4. RSF12 is CLB5. The clb5 swi4 mutant cells arrest at G2/M due to the activation of the DNA-damage checkpoint. Defects in DNA integrity was confirmed by the increased rates of chromosome loss and mitotic recombination. Other results suggest the presence of additional defects related to morphogenesis. Interestingly, genes of the PKC pathway rescue the growth defect of clb5 swi4, and pkc1 and slt2 mutations are synthetic lethal with clb5, pointing to a connection between Clb5, the PKC pathway, and Swi4. Different observations suggest that like Clb5, the PKC pathway and Swi4 are in…

Saccharomyces cerevisiae ProteinsMitotic crossoverBlotting WesternMutantSaccharomyces cerevisiaeSaccharomyces cerevisiaeInvestigationsCyclin BBiologymedicine.disease_causeGeneticsmedicineHydroxyureaImmunoprecipitationDNA FungalFluorescent Antibody Technique IndirectTranscription factorProtein Kinase CProtein kinase CCyclinRecombination GeneticGeneticsMutationKinaseCell CyclefungiFlow Cytometrybiology.organism_classificationMolecular biologyCell biologyDNA-Binding ProteinsMutationChromosomes FungalTranscription FactorsGenetics
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Physical and Genetic Interactions Link the Yeast Protein Zds1p with mRNA Nuclear Export

2005

Eukaryotic gene expression requires the export of mRNA from the nucleus to the cytoplasm. The DEAD box protein Dbp5p is an essential export factor conserved from yeast to man. A fraction of Dbp5p forms a complex with nucleoporins of the cytoplasmic filaments of the nuclear pore complex. Gfd1p was identified originally as a multicopy suppressor of the rat8-2 ts allele of DBP5. Here we reported that Dbp5p and Gfd1p interact with Zds1p, a protein previously identified as a multicopy suppressor in several yeast genetic screens. By using the two-hybrid system, we showed that Zds1p interacts in vivo with both Gfd1p and Dbp5p. In vitro binding experiments revealed that Gfd1p and Dbp5p bind directl…

Saccharomyces cerevisiae ProteinsMolecular Sequence DataMutantActive Transport Cell NucleusSaccharomyces cerevisiaeBiologyBiochemistryCytosolGene expressionmedicineRNA MessengerNuclear poreNuclear export signalMolecular BiologyAdaptor Proteins Signal TransducingDNA PrimersGeneticsMessenger RNABase SequenceNuclear cap-binding protein complexRNA FungalCell BiologyCell biologyCell nucleusmedicine.anatomical_structureNucleoporinGenome FungalJournal of Biological Chemistry
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HAT1 and HAT2 Proteins Are Components of a Yeast Nuclear Histone Acetyltransferase Enzyme Specific for Free Histone H4

1998

We have analyzed the histone acetyltransferase enzymes obtained from a series of yeast hat1, hat2, and gcn5 single mutants and hat1,hat2 and hat1,gcn5 double mutants. Extracts prepared from both hat1 and hat2 mutant strains specifically lack the following two histone acetyltransferase activities: the well known cytoplasmic type B enzyme and a free histone H4-specific histone acetyltransferase located in the nucleus. The catalytic subunits of both cytoplasmic and nuclear enzymes have identical molecular masses (42 kDa), the same as that of HAT1. However, the cytoplasmic complex has a molecular mass (150 kDa) greater than that of the nuclear complex (110 kDa). The possible functions of HAT1 a…

Saccharomyces cerevisiae ProteinsMolecular Sequence DataSaccharomyces cerevisiaeBiologyBiochemistryCatalysisSubstrate SpecificityHistonesHistone H4Histone H1AcetyltransferasesHistone H2AHistone octamerMolecular BiologyHistone AcetyltransferasesCell NucleusHistone AcetyltransferasesBase SequenceAcetylationCell BiologyHistone acetyltransferaseMolecular WeightPhenotypeOligodeoxyribonucleotidesBiochemistryMutagenesisHistone methyltransferasebiology.proteinHAT1Journal of Biological Chemistry
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Global translational repression induced by iron deficiency in yeast depends on the Gcn2/eIF2α pathway

2020

Iron is an essential element for all eukaryotic organisms because it participates as a redox active cofactor in a wide range of biological processes, including protein synthesis. Translation is probably the most energy consuming process in cells. Therefore, one of the initial responses of eukaryotic cells to stress or nutrient limitation is the arrest of mRNA translation. In first instance, the budding yeast Saccharomyces cerevisiae responds to iron deficiency by activating iron acquisition and remodeling cellular metabolism in order to prioritize essential over non-essential iron-dependent processes. We have determined that, despite a global decrease in transcription, mRNA translation is a…

Saccharomyces cerevisiae ProteinsMolecular biologyEukaryotic Initiation Factor-2Saccharomyces cerevisiaelcsh:MedicineSaccharomyces cerevisiaeProtein Serine-Threonine KinasesBiochemistryArticleCofactorTranscription (biology)Protein biosynthesislcsh:SciencePsychological repressionMultidisciplinarybiologyChemistrylcsh:RTranslation (biology)Iron Deficienciesbiology.organism_classificationYeastCell biologyProtein BiosynthesisTransfer RNAbiology.proteinlcsh:Q
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Regulation of mating in the budding yeast Saccharomyces cerevisiae by the zinc cluster proteins Sut1 and Sut2

2013

This article is made available through the Brunel Open Access Publishing Fund. Copyright @ The Authors. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. The zinc cluster proteins Sut1 and Sut2 play a role in sterol uptake and filamentous growth in the budding yeast Saccharomyces cerevisiae. In this study, we show that they are also involved in mating. Cells that lack both SUT1 and SUT2 were defective in mating. The expression of the genes NCE102 and PRR2 was increased in the sut1 sut2 double deletion mutant…

Saccharomyces cerevisiae ProteinsMonosaccharide Transport ProteinsSaccharomyces cerevisiaeBiophysicsSaccharomyces cerevisiaeBiologyBiochemistryFungal ProteinsGene Expression Regulation FungalReproduction AsexualBudding yeastMatingMolecular BiologyGenereproductive and urinary physiologyGeneticsMatingZinc FingersCell Biologybiology.organism_classificationBudding yeastSut2Sut1Mating of yeastPheromone responseZinc cluster proteinsZinc Clusterbehavior and behavior mechanismsPheromoneTranscription FactorsSterol uptakeBiochemical and Biophysical Research Communications
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The three trehalases Nth1p, Nth2p and Ath1p participate in the mobilization of intracellular trehalose required for recovery from saline stress in Sa…

2009

Trehalose accumulation is a common response to several stresses in the yeast Saccharomyces cerevisiae. This metabolite protects proteins and membrane lipids from structural damage and helps cells to maintain integrity. Based on genetic studies, degradation of trehalose has been proposed as a required mechanism for growth recovery after stress, and the neutral trehalase Nth1p as the unique degradative activity involved. Here we constructed a collection of mutants for several trehalose metabolism and transport genes and analysed their growth and trehalose mobilization profiles during experiments of saline stress recovery. The behaviour of the triple ¿nth1¿nth2¿ath1 and quadruple ¿nth1¿nth2¿at…

Saccharomyces cerevisiae ProteinsMonosaccharide Transport ProteinsSymportersMutantSaccharomyces cerevisiaeGenes FungalTrehaloseMetabolismSaccharomyces cerevisiaeBiologybiology.organism_classificationMicrobiologyTrehaloseYeastchemistry.chemical_compoundBiochemistrychemistryStress PhysiologicalSymporterTrehalaseTrehalaseIntracellularGene DeletionMicrobiology (Reading, England)
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Functional distinction between Cln1p and Cln2p cyclins in the control of the Saccharomyces cerevisiae mitotic cycle.

2004

Abstract Cln1p and Cln2p are considered as equivalent cyclins on the basis of sequence homology, regulation, and functional studies. Here we describe a functional distinction between the Cln1p and Cln2p cyclins in the control of the G1/S transition. Inactivation of CLN2, but not of CLN1, leads to a larger-than-normal cell size, whereas overexpression of CLN2, but not of CLN1, results in smaller-than-normal cells. Furthermore, mild ectopic expression of CLN2, but not of CLN1, suppresses the lethality of swi4swi6 and cdc28 mutant strains. In the absence of Cln1p, the kinetics of budding, initiation of DNA replication, and activation of the Start-transcription program are not affected; by cont…

Saccharomyces cerevisiae ProteinsMutantSaccharomyces cerevisiaeBlotting WesternMitosisSaccharomyces cerevisiaeBiologyInvestigationsmedicine.disease_causeS PhaseCyclinsGeneticsmedicineImmunoprecipitationFluorescent Antibody Technique IndirectMitosisCyclinCell SizeGeneticsCyclin-dependent kinase 1MutationDNA replicationbiology.organism_classificationBlotting NorthernBridged Bicyclo Compounds HeterocyclicFlow CytometryMolecular biologyThiazolesMutationThiazolidinesEctopic expressionGenetics
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Blockage of cell wall receptors for yeast killer toxin KT28 with antimannoprotein antibodies.

1990

Binding of yeast killer toxin KT28 to its primary cell wall receptor was specifically blocked with polyclonal antimannoprotein antibodies which masked all toxin-binding sites on the surface of sensitive yeast cells. By indirect immunofluorescence, it was shown that KT28 binds to the cell wall mannoprotein and that the toxin resistance of mannoprotein mutants (mnn) of Saccharomyces cerevisiae was due to a lack of killer toxin-binding sites within the yeast cell wall. Structural analysis of acetylated mannoprotein from KT28-resistant mutant strains identified the outer mannotriose side chains as the actual killer toxin-binding domains.

Saccharomyces cerevisiae ProteinsMutantSaccharomyces cerevisiaeFluorescent Antibody TechniqueSaccharomyces cerevisiaeBiologymedicine.disease_causeAntibodiesCell wallCell WallmedicinePharmacology (medical)ReceptorPharmacologyMembrane GlycoproteinsToxinMycotoxinsbiology.organism_classificationYeastKiller Factors YeastCell biologycarbohydrates (lipids)Infectious DiseasesBiochemistryPolyclonal antibodiesbiology.proteinAntibodyResearch Article
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