Search results for "G proteins"

showing 10 items of 992 documents

Energetic aspects of intramolecular coupling between the nucleotide binding site and the distal switch II region of the yeast RAS2 protein

1994

AbstractWe have studied the interaction of the yeast RAS2 protein with guanine nucleotides using energetic parameters for the dissociation of RAS·nucleotide complexes. The results indicated that a Gly → Ser substitution at position 82 led to an altered interaction with GppNHp and, to a lesser extent, also with GDP. It was also possible to conclude that structural perturbation of Gly82 can stimulate nucleotide release by decreasing the energetic barrier for nucleotide dissociation. This, together with the observation that residues 80 and 81 are involved in the response of RAS to nucleotide exchange factors without affecting GDP binding per se, suggests a potential mechanism for exchange fact…

Saccharomyces cerevisiae ProteinsStereochemistryCdc25GuanineSaccharomyces cerevisiaeGlycineBiophysicsSaccharomyces cerevisiaeGuanosine DiphosphateBiochemistryFungal ProteinsStructure-Activity RelationshipSCD25chemistry.chemical_compoundGTP-Binding ProteinsStructural BiologyEscherichia coliSerineGeneticsNucleotideBinding siteRas2Molecular Biologychemistry.chemical_classificationGuanylyl ImidodiphosphateBinding SitesCDC25biologyGDP bindingTemperatureCell Biologybiology.organism_classificationGuanine NucleotidesRecombinant ProteinsYeastchemistryras ProteinsGDP exchange factorbiology.proteinThermodynamicsRASFEBS Letters
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A short-range gradient of histone H3 acetylation and Tup1p redistribution at the promoter of the Saccharomyces cerevisiae SUC2 gene.

2003

Chromatin immunoprecipitation assays are used to map H3 and H4 acetylation over the promoter nucleosomes and the coding region of the Saccharomyces cerevisiae SUC2 gene, under repressed and derepressed conditions, using wild type and mutant strains. In wild type cells, a high level of H3 acetylation at the distal end of the promoter drops sharply toward the proximal nucleosome that covers the TATA box, a gradient that become even steeper on derepression. In contrast, substantial H4 acetylation shows no such gradient and extends into the coding region. Overall levels of both H3 and H4 acetylation rise on derepression. Mutation of GCN5 or SNF2 lead to substantially reduced SUC2 expression; in…

Saccharomyces cerevisiae ProteinsTATA boxMutantGene ExpressionSaccharomyces cerevisiaeBiologyBiochemistryPolymerase Chain ReactionHistonesNucleosomeRNA MessengerHistone H3 acetylationDNA FungalPromoter Regions GeneticMolecular BiologyDerepressionHistone AcetyltransferasesAdenosine Triphosphatasesbeta-FructofuranosidaseWild typeChromosome MappingNuclear ProteinsCell BiologyMolecular biologyDNA-Binding ProteinsRepressor ProteinsAcetylationMutagenesisChromatin immunoprecipitationProtein KinasesTranscription FactorsThe Journal of biological chemistry
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Unveiling novel interactions of histone chaperone Asf1 linked to TREX-2 factors Sus1 and Thp1

2014

13 páginas, 7 figuras, 2 yablas

Saccharomyces cerevisiae ProteinsTranscription Genetic(5-10) yAsf1Histone H2B ubiquitinationCell Cycle ProteinsSAGASaccharomyces cerevisiaeBiologyyeastMethylationTREX-2RNA TransportHistonesSus1Histone H3Histone H1Gene Expression Regulation FungalhistonesHistone H2ANucleosomeHistone codeTAP-MS strategyHistone ChaperonesRNA MessengerHistone octamerGeneticsNuclear ProteinsRNA-Binding ProteinsAcetylationCell BiologyYeastCell biologyRibonucleoproteinsHistone methyltransferaseProtein Processing Post-TranslationalMolecular ChaperonesResearch Paper
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Saccharomyces cerevisiae Glutaredoxin 5-deficient Cells Subjected to Continuous Oxidizing Conditions Are Affected in the Expression of Specific Sets …

2004

The Saccharomyces cerevisiae GRX5 gene codes for a mitochondrial glutaredoxin involved in the synthesis of iron/sulfur clusters. Its absence prevents respiratory growth and causes the accumulation of iron inside cells and constitutive oxidation of proteins. Null ⌬grx5 mu- tants were used as an example of continuously oxidized cells, as opposed to situations in which oxidative stress is instantaneously caused by addition of external oxi- dants. Whole transcriptome analysis was carried out in the mutant cells. The set of genes whose expression was affected by the absence of Grx5 does not significantly overlap with the set of genes affected in respiratory petite mutants. Many Aft1-dependent ge…

Saccharomyces cerevisiae ProteinsTranscription GeneticIronSaccharomyces cerevisiaeMutantProtein Array AnalysisDown-RegulationSaccharomyces cerevisiaeOxidative phosphorylationmedicine.disease_causeProtein oxidationBiochemistryOxygen ConsumptionGene Expression Regulation FungalIron-Binding ProteinsGlutaredoxinmedicineRNA MessengerMolecular BiologyGlutaredoxinsbiologyMembrane ProteinsNuclear ProteinsProteinsRNA-Binding ProteinsCell BiologyBlotting Northernbiology.organism_classificationCarbonUp-RegulationOxygenOxidative StressRegulonCCAAT-Binding FactorDatabases as TopicBiochemistryMutationFrataxinbiology.proteinOxidoreductasesReactive Oxygen SpeciesOxidative stressTranscription FactorsJournal of Biological Chemistry
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Rpb4 and Puf3 imprint and post-transcriptionally control the stability of a common set of mRNAs in yeast

2020

ABSTRACTGene expression involving RNA polymerase II is regulated by the concerted interplay between mRNA synthesis and degradation, crosstalk in which mRNA decay machinery and transcription machinery respectively impact transcription and mRNA stability. Rpb4, and likely dimer Rpb4/7, seem the central components of the RNA pol II governing these processes. In this work we unravel the molecular mechanisms participated by Rpb4 that mediate the posttranscriptional events regulating mRNA imprinting and stability. By RIP-Seq, we analyzed genome-wide the association of Rpb4 with mRNAs and demonstrated that it targeted a large population of more than 1400 transcripts. A group of these mRNAs was als…

Saccharomyces cerevisiae ProteinsTranscription GeneticRNA StabilityRNA polymerase IIRNA-binding proteinSaccharomyces cerevisiaeGenomic Imprinting03 medical and health sciences0302 clinical medicineTranscription (biology)Gene Expression Regulation FungalGene expressionRNA MessengerRNA Processing Post-TranscriptionalImprinting (psychology)Molecular Biology030304 developmental biology0303 health sciencesMessenger RNABinding SitesbiologyChemistryRNA-Binding ProteinsMolecular Sequence AnnotationCell BiologyChromatinChromatinCell biologyCrosstalk (biology)030220 oncology & carcinogenesisbiology.proteinRNA Polymerase IIProtein BindingResearch PaperRNA Biology
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Hyperphosphorylation of Msn2p and Msn4p in response to heat shock and the diauxic shift is inhibited by cAMP in Saccharomyces cerevisiae.

2000

In response to various stresses, as well as during the diauxic transition, the Msn2p and Msn4p transcription factors of Saccharomyces cerevisiae are activated and induce a large set of genes. This activation is inhibited by the Ras/cAMP/PKA (cAMP-dependent protein kinase) pathway. Here we show by immunoblotting experiments that Msn2p and Msn4p are phosphorylated in vivo during growth on glucose, and become hyperphosphorylated at the diauxic transition and upon heat shock. This hyperphosphorylation is correlated with activation of Msn2/4p-dependent transcription. An increased level of cAMP prevents and reverses these hyperphosphorylations, indicating that kinases other than PKA are involved.…

Saccharomyces cerevisiae ProteinsbiologyKinaseSaccharomyces cerevisiaeImmunoblottingHyperphosphorylationSaccharomyces cerevisiaebiology.organism_classificationAlkaline PhosphataseMicrobiologyCyclic AMP-Dependent Protein KinasesCell biologyDNA-Binding ProteinsBiochemistryTranscription (biology)Gene Expression Regulation FungalCyclic AMPPhosphorylationHeat shockPhosphorylationProtein kinase ATranscription factorHeat-Shock ResponseTranscription FactorsMicrobiology (Reading, England)
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Hif1 Is a Component of Yeast Histone Acetyltransferase B, a Complex Mainly Localized in the Nucleus

2004

Hat1 is the catalytic subunit of the only type B histone acetyltransferase known (HAT-B). The enzyme specifically acetylates lysine 12, and to a lesser extent lysine 5, of free, non-chromatin-bound histone H4. The complex is usually isolated with cytosolic fractions and is thought to be involved in chromatin assembly. The Saccharomyces cerevisiae HAT-B complex also contains Hat2, a protein stimulating Hat1 catalytic activity. We have now identified by two-hybrid experiments Hif1 as both a Hat1- and a histone H4-interacting protein. These interactions were dependent on HAT2, indicating a mediating role for Hat2. Biochemical fractionation and co-immunoprecipitation assays demonstrated that Hi…

Saccharomyces cerevisiae ProteinsbiologyNuclear ProteinsAcetylationSaccharomyces cerevisiaeCell BiologyHistone acetyltransferaseTelomereBiochemistryDNA-Binding ProteinsHistonesHistone H4HistoneBiochemistryAcetyltransferasesHistone methyltransferaseHistone H2Abiology.proteinHistone codeHypoxia-Inducible Factor 1Histone octamerHAT1Molecular BiologyHistone AcetyltransferasesTranscription FactorsJournal of Biological Chemistry
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The Lsm1-7/Pat1 complex binds to stress-activated mRNAs and modulates the response to hyperosmotic shock.

2018

RNA-binding proteins (RBPs) establish the cellular fate of a transcript, but an understanding of these processes has been limited by a lack of identified specific interactions between RNA and protein molecules. Using MS2 RNA tagging, we have purified proteins associated with individual mRNA species induced by osmotic stress, STL1 and GPD1. We found members of the Lsm1-7/Pat1 RBP complex to preferentially bind these mRNAs, relative to the non-stress induced mRNAs, HYP2 and ASH1. To assess the functional importance, we mutated components of the Lsm1-7/Pat1 RBP complex and analyzed the impact on expression of osmostress gene products. We observed a defect in global translation inhibition under…

Saccharomyces cerevisiae Proteinslcsh:QH426-470Gene ExpressionSaccharomyces cerevisiaeBiochemistryOsmotic PressureOsmotic ShockGeneticsRNA MessengerCellular Stress ResponsesGlycerol-3-Phosphate Dehydrogenase (NAD+)Biology and life sciencesMessenger RNAMembrane Transport ProteinsRNA-Binding ProteinsProteinsCell BiologyRepressor ProteinsNucleic acidslcsh:GeneticsRibonucleoproteinsRNA Cap-Binding ProteinsCell ProcessesProtein BiosynthesisPolyribosomesRNAProtein TranslationCellular Structures and OrganellesRibosomesProtein BindingResearch ArticlePLoS genetics
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Targeting Homer genes using adeno-associated viral vector: lessons learned from behavioural and neurochemical studies.

2008

Over a decade of in-vitro data support a critical role for members of the Homer family of postsynaptic scaffolding proteins in regulating the functional architecture of glutamate synapses. Earlier studies of Homer knockout mice indicated a necessary role for Homer gene products in normal mesocorticolimbic glutamate transmission and behaviours associated therewith. The advent of adeno-associated viral vectors carrying cDNA for, or short hairpin RNA against, specific Homer isoforms enabled the site-directed targeting of Homers to neurons in the brain. This approach has allowed our groups to address developmental issues associated with conventional knockout mice, to confirm active roles for di…

Scaffold proteinSubstance-Related DisordersTransgeneEmotionsGenetic VectorsGlutamic AcidMice TransgenicBiologySynaptic TransmissionArticleViral vectorAdenoviridaeSmall hairpin RNAMiceNeurochemicalHomer Scaffolding ProteinsAnimalsGeneGenes Immediate-EarlyPharmacologyMice KnockoutBehavior AnimalGlutamate receptorGene Transfer TechniquesBrainPsychiatry and Mental healthAlcoholismKnockout mouseMutagenesis Site-DirectedArousalCarrier ProteinsNeuroscienceBehavioural pharmacology
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IRSp53 controls plasma membrane shape and polarized transport at the nascent lumen in epithelial tubules.

2020

It is unclear whether the establishment of apical–basal cell polarity during the generation of epithelial lumens requires molecules acting at the plasma membrane/actin interface. Here, we show that the I-BAR-containing IRSp53 protein controls lumen formation and the positioning of the polarity determinants aPKC and podocalyxin. Molecularly, IRSp53 acts by regulating the localization and activity of the small GTPase RAB35, and by interacting with the actin capping protein EPS8. Using correlative light and electron microscopy, we further show that IRSp53 ensures the shape and continuity of the opposing plasma membrane of two daughter cells, leading to the formation of a single apical lumen. G…

ScienceSialoglycoproteinsQCell MembraneCell PolarityEpithelial CellsNerve Tissue ProteinsApicobasal polaritySettore MED/08 - Anatomia PatologicaActins Cell Membrane Cell Polarity Epithelial Cells Female Morphogenesis Nerve Tissue Proteins Protein Transport Sialoglycoproteins rab GTP-Binding ProteinsActinsArticleProtein Transportrab GTP-Binding ProteinsMorphogenesisHumanslcsh:QFemalelcsh:ScienceNature communications
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