Search results for "G proteins"

showing 10 items of 992 documents

Yeast gene CMR1/YDL156W is consistently co-expressed with genes participating in DNA-metabolic processes in a variety of stringent clustering experim…

2013

© 2013 The Authors. Published by the Royal Society under the terms of the Creative Commons Attribution License http://creativecommons.org/licenses/by/3.0/, which permits unrestricted use, provided the original author and source are credited. The binarization of consensus partition matrices (Bi-CoPaM) method has, among its unique features, the ability to perform ensemble clustering over the same set of genes from multiple microarray datasets by using various clustering methods in order to generate tunable tight clusters. Therefore, we have used the Bi-CoPaM method to the most synchronized 500 cell-cycle-regulated yeast genes from different microarray datasets to produce four tight, specific …

Saccharomyces cerevisiae ProteinsCMR1/YDL156W1004Biomedical EngineeringBiophysicsG1/S transitionDNA repairBioengineeringDNA-Directed DNA PolymeraseSaccharomyces cerevisiaeBiologyDNA replication2244BiochemistryYeast geneBiomaterialschemistry.chemical_compoundReplication Protein Abinarization of consensus partition matrixCluster AnalysisCluster analysisGeneDNA-directed DNA polymeraseLicenseResearch Articlesta113GeneticsModels GeneticGene Expression ProfilingDNACreative commonsMicroarray AnalysisDNA-Binding ProteinsGenes cdcGene expression profilingchemistryDNABiotechnology
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Role of glycine-82 as a pivot point during the transition from the inactive to the active form of the yeast Ras2 protein

1991

AbstractRas proteins bind either GDP or GTP with high affinity. However, only the GTP-bound form of the yeast Ras2 protein is able to stimulate adenylyl cyclase. To identify amino acid residues that play a role in the conversion from the GDP-bound to the GTP-bound state of Ras proteins, we have searched for single amino acid substitutions that selectively affected the binding of one of the two nucleotides. We have found that the replacement of glycine-82 of the Ras2 protein by serine resulted in an increased rate of dissociation of Gpp(NH)p, a nonhydrolysable analog of GTP, while the GDP dissociation rate was not significantly modified. Glycine-82 resides in a region that is highly conserve…

Saccharomyces cerevisiae ProteinsGTP'Guanosine diphosphateProtein ConformationRestriction MappingGlycineBiophysicsSaccharomyces cerevisiaeBiochemistryFungal ProteinsGTP-binding protein regulatorsProtein structureGTP-Binding ProteinsStructural BiologyEscherichia coliGeneticsRHO protein GDP dissociation inhibitorAmino Acid SequenceRas2Binding siteMolecular BiologyPeptide sequencechemistry.chemical_classificationGuanylyl ImidodiphosphateBinding SitesPoint mutationChemistryCell BiologyGuanosine triphosphateRecombinant ProteinsAmino acidModels StructuralBiochemistryMutagenesis Site-Directedras ProteinsS. cerevisaePlasmidsRasFEBS Letters
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Response of the Saccharomyces cerevisiae Mpk1 Mitogen-Activated Protein Kinase Pathway to Increases in Internal Turgor Pressure Caused by Loss of Ppz…

2004

ABSTRACT The Mpk1 pathway of Saccharomyces cerevisiae is a key determinant of cell wall integrity. A genetic link between the Mpk1 kinase and the Ppz phosphatases has been reported, but the nature of this connection was unclear. Recently, the Ppz phosphatases were shown to be regulators of K + and pH homeostasis. Here, we demonstrate that Ppz-deficient strains display increased steady-state K + levels and sensitivity to increased KCl concentrations. Given these observations and the fact that K + is the major determinant of intracellular turgor pressure, we reasoned that the connection between PPZ1 and - 2 and MPK1 was due to the combination of increased internal turgor pressure in Ppz-defic…

Saccharomyces cerevisiae ProteinsGenotypeTranscription GeneticBlotting WesternTurgor pressureSaccharomyces cerevisiaePhosphataseSaccharomyces cerevisiaeMicrobiologyArticlePheromonesPotassium ChlorideCell wallPhosphoprotein PhosphatasesSorbitolPhosphorylationMolecular BiologyMembrane GlycoproteinsbiologyKinaseCalcium-Binding ProteinsIntracellular Signaling Peptides and ProteinsTemperatureMembrane ProteinsGeneral MedicineHydrogen-Ion ConcentrationBlotting Northernbiology.organism_classificationUp-RegulationPhenotypeBiochemistryMitogen-activated protein kinaseMutationPotassiumbiology.proteinPhosphorylationMitogen-Activated Protein KinasesIntracellularEukaryotic Cell
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Performance of industrial strains of Saccharomyces cerevisae during wine fermentation is affected by manipulation strategies based on sporulation.

2002

Genetic manipulation of industrial wine yeast strains has become an essential tool for both the study of the molecular mechanisms underlaying their physiology and the improvement of their fermentative properties. The construction of null mutants for any gene in these usually diploid strains, by using a procedure based on sporulation of a heterozygote lacking one copy of the gene of interest, has been tested as an alternative to the tedious work of sequential disruption of the complete set of copies. Our results indicate that most of the homozygotes resulting from sporulation of wine yeast strains are defective in glucose consumption under microvinification conditions in synthetic must and p…

Saccharomyces cerevisiae ProteinsGlycoside HydrolasesMutantWineSaccharomyces cerevisiaeBiologyApplied Microbiology and BiotechnologyMicrobiologyDNA FungalGeneEcology Evolution Behavior and SystematicsGeneticsWineFermentation in winemakingbeta-FructofuranosidaseWild typeFungal geneticsfood and beveragesSpores FungalDNA-Binding ProteinsRepressor ProteinsYeast in winemakingBlotting SouthernGlucoseFermentationFermentationPlasmidsSystematic and applied microbiology
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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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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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Convergence of the target of rapamycin and the Snf1 protein kinase pathways in the regulation of the subcellular localization of Msn2, a transcriptio…

2002

The subcellular localization of Msn2, a transcriptional activator of STRE (stress response element)-regulated genes, is modulated by carbon source availability. In cells growing in glucose, Msn2 is located mainly in the cytosol, whereas in carbon source-starved cells, Msn2 is located largely inside the nucleus. However, in cells lacking Reg1 (the regulatory subunit of the Reg1/Glc7 protein phosphatase complex), the regulation of subcellular distribution is absent, Msn2 being constitutively present in the cytosol. The localization defect in these mutants is specific for carbon starvation stress, and it is because of the presence of an abnormally active Snf1 protein kinase that inhibits the n…

Saccharomyces cerevisiae ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeMitogen-activated protein kinase kinaseBiologyProtein Serine-Threonine KinasesBiochemistryASK1Molecular BiologyDNA PrimersSirolimusMAP kinase kinase kinaseBase SequenceKinaseCell BiologySubcellular localizationCarbonCell biologyCulture MediaDNA-Binding ProteinsCytosolBiochemistryTrans-ActivatorsCyclin-dependent kinase 9Nuclear localization sequenceSubcellular FractionsTranscription FactorsThe Journal of biological chemistry
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The yeast histone acetyltransferase A2 complex, but not free Gcn5p, binds stably to nucleosomal arrays.

2000

We have investigated the structural basis for the differential catalytic function of the yeast Gcn5p-containing histone acetyltransferase (HAT) A2 complex and free recombinant yeast Gcn5p (rGcn5p). HAT A2 is shown to be a unique complex that contains Gcn5p, Ada2p, and Ada3p, but not proteins specific to other related HAT A complexes, e.g. ADA, SAGA. Nevertheless, HAT A2 produces the same unique polyacetylation pattern of nucleosomal substrates reported previously for ADA and SAGA, demonstrating that proteins specific to the ADA and SAGA complexes do not influence the enzymatic activity of Gcn5p within the HAT A2 complex. To investigate the role of substrate interactions in the differential …

Saccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeBiologyBiochemistrySubstrate SpecificityFungal ProteinsHistonesTetramerAcetyl Coenzyme AAcetyltransferasesparasitic diseasesCentrifugation Density GradientAnimalsMolecular BiologyHistone Acetyltransferaseschemistry.chemical_classificationSubstrate (chemistry)AcetylationCell BiologyHistone acetyltransferaseYeastChromatinRecombinant ProteinsTrypsinizationNucleosomesN-terminusDNA-Binding Proteinsenzymes and coenzymes (carbohydrates)EnzymechemistryBiochemistryAcetylationBiophysicsbiology.proteinChickensProtein KinasesThe Journal of biological chemistry
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Trx2p-dependent Regulation of Saccharomyces cerevisiae Oxidative Stress Response by the Skn7p Transcription Factor under Respiring Conditions

2013

The whole genome analysis has demonstrated that wine yeasts undergo changes in promoter regions and variations in gene copy number, which make them different to lab strains and help them better adapt to stressful conditions during winemaking, where oxidative stress plays a critical role. Since cytoplasmic thioredoxin II, a small protein with thiol-disulphide oxidoreductase activity, has been seen to perform important functions under biomass propagation conditions of wine yeasts, we studied the involvement of Trx2p in the molecular regulation of the oxidative stress transcriptional response on these strains. In this study, we analyzed the expression levels of several oxidative stress-related…

Saccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeBlotting WesternMolecular Sequence Datalcsh:MedicineWineOxidative phosphorylationSaccharomyces cerevisiaemedicine.disease_causePolymerase Chain ReactionThioredoxinsGene Expression Regulation FungalGene expressionmedicineImmunoprecipitationPhosphorylationlcsh:ScienceTranscription factorHeat-shock responseDNA PrimersRegulation of gene expressionMultidisciplinarybiologyBase Sequencelcsh:RPromoterbiology.organism_classificationCatalasebeta-GalactosidaseYeastGene regulationDNA-Binding ProteinsOxidative StressBiochemistryOxidative stresslcsh:QGene expressionThioredoxinTranscription factorOxidative stressGene DeletionResearch ArticlePlasmidsTranscription FactorsPLoS ONE
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