Search results for "histone acetyltransferases"

showing 10 items of 44 documents

Histone deacetylase inhibitors induce in human hepatoma HepG2 cells acetylation of p53 and histones in correlation with apoptotic effects

2007

This report shows that histone deacetylase inhibitors (HDACIs) induced apoptosis in human hepatoma HepG2 cells in a dose- and time-dependent manner. Trichostatin A (TSA), ITF2357 and suberoylanilide hydroxamic acid (SAHA), which were very effective agents, caused apoptotic effects after a lag phase of 12-16 h. In order to elucidate the mechanism of HDACIs action in HepG2 cells we have studied the effects of TSA, ITF2357 and SAHA on acetylation of p53 and histones H2A, H2B, H3 and H4. It was observed that HDACIs rapidly induced acetylation of these proteins, being the effects clearly visible already at 30 min of treatment at the same doses which caused apoptosis. Analysis of the immunocomple…

Cancer ResearchProgrammed cell deathCarcinoma Hepatocellularmedicine.drug_classAntineoplastic AgentsApoptosisBiologyHydroxamic AcidsHistonesCell Line TumorSettore BIO/10 - BiochimicamedicineHumansBenzothiazolesEnzyme InhibitorsRNA Small InterferingHistone AcetyltransferasesVorinostatHistone deacetylase inhibitors acetylation p53 histones apoptosis hepatoma cells.Liver NeoplasmsHistone deacetylase inhibitorAcetylationProto-Oncogene Proteins c-mdm2Molecular biologyHistone Deacetylase InhibitorsTrichostatin AHistoneOncologyPCAFAcetylationbiology.proteinHistone deacetylaseTumor Suppressor Protein p53DNA DamageToluenemedicine.drugInternational Journal of Oncology
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Subcellular localization and nucleosome specificity of yeast histone acetyltransferases

1991

We have previously reported [López-Rodas et al. (1989) J. Biol. Chem. 264, 19028-19033] that the yeast Saccharomyces cerevisiae contains four histone acetyltransferases, which can be resolved by ion-exchange chromatography, and their specificity toward yeast free histones was studied. In the present contribution we show that three of the enzymes are nuclear, type A histone acetyltransferases and they are able to acetylate nucleosome-bound histones. They differ in their histone specificity. Enzyme A1 acetylates H2A in chicken nucleosomes, although it is specific for yeast free H2B; histone acetyltransferase A2 is highly specific for H3, and histone acetyltransferase A3 preparations acetylate…

Cell NucleusHistone AcetyltransferasesSaccharomyces cerevisiae ProteinsbiologySaccharomyces cerevisiaeHistone acetyltransferaseChromatography Ion ExchangeBiochemistryAmidohydrolasesNucleosomesSubstrate SpecificityHistonesBiochemistryHistone H1AcetyltransferasesHistone methylationHistone H2Abiology.proteinHistone codeHistone octamerHistone deacetylase activityHistone AcetyltransferasesBiochemistry
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Chromatin dynamics of the developmentally regulated P. lividus neural alpha tubulin gene

2011

Over 40 years ago, Allfrey and colleagues (1964) suggested that two histone modifications, namely acetylation and methylation, might regulate RNA synthesis. Nowadays it is universally accepted that activation of gene expression strictly depends on enzymatic mechanisms able to dynamically modify chromatin structure. Here, using techniques including DNaseI hypersensitive site analysis, chomatin immunoprecipitation and quantitative PCR analysis, we have analyzed the dynamics of histone post-translation modifications involved in developmentally/spatially controlled activation of the sea urchin PlTalpha2 tubulin gene. We have demonstrated that only when the PlTalpha2 core promoter chromatin is a…

Chromatin ImmunoprecipitationEmbryologyRNA polymerase IISettore BIO/11 - Biologia MolecolareMethylationNervous SystemHistone DeacetylasesHistonesTubulinGene expressionAnimalsParacentrotus lividus chromatin modification epigenetic reprogramming nervous systemPromoter Regions GeneticHistone AcetyltransferasesEpigenomicsHistone DemethylasesbiologyGene Expression Regulation DevelopmentalAcetylationPromoterHistone-Lysine N-MethyltransferaseMolecular biologyChromatinChromatinCell biologyHistoneAcetylationHistone MethyltransferasesParacentrotusbiology.proteinRNA Polymerase IIProtein Processing Post-TranslationalHypersensitive siteDevelopmental Biology
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Epigenetic Transcriptional Regulation of the Growth Arrest-Specific gene 1 (Gas1) in Hepatic Cell Proliferation at Mononucleosomal Resolution

2011

Background Gas1 (growth arrest-specific 1) gene is known to inhibit cell proliferation in a variety of models, but its possible implication in regulating quiescence in adult tissues has not been examined to date. The knowledge of how Gas1 is regulated in quiescence may contribute to understand the deregulation occurring in neoplastic diseases. Methodology/Principal Findings Gas1 expression has been studied in quiescent murine liver and during the naturally synchronized cell proliferation after partial hepatectomy. Chromatin immunoprecipitation at nucleosomal resolution (Nuc-ChIP) has been used to carry out the study preserving the in vivo conditions. Transcription has been assessed at real …

Chromatin ImmunoprecipitationTranscription GeneticGene Expressionlcsh:MedicineCell Cycle ProteinsRNA polymerase IIBiologyGPI-Linked ProteinsMethylationHistone DeacetylasesChromatin remodelingEpigenesis GeneticS PhaseHistonesMiceMolecular Cell BiologyTranscriptional regulationAnimalsHepatectomyEpigeneticsPromoter Regions Geneticlcsh:ScienceBiologyCell ProliferationHistone AcetyltransferasesRegulation of gene expressionMultidisciplinaryReverse Transcriptase Polymerase Chain ReactionGene Expression Profilinglcsh:RG1 PhaseAcetylationHistone ModificationImmunohistochemistryMolecular biologyChromatinNucleosomesChromatinHistoneGene Expression RegulationLiverbiology.proteinlcsh:QTranscription Initiation SiteChromatin immunoprecipitationProtein BindingResearch ArticlePLoS ONE
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'Up-regulation of histone acetylation induced by social defeat mediates the conditioned rewarding effects of cocaine

2016

Social defeat (SD) induces a long-lasting increase in the rewarding effects of psychostimulants measured using the self-administration and conditioned place procedures (CPP). However, little is known about the epigenetic changes induced by social stress and about their role in the increased response to the rewarding effects of psychostimulants. Considering that histone acetylation regulates transcriptional activity and contributes to drug-induced behavioral changes, we addressed the hypothesis that SD induces transcriptional changes by histone modifications associated with the acquisition of place conditioning. After a fourth defeat, H3(K9) acetylation was decreased in the hippocampus, whil…

Dominance-SubordinationMaleCurcuminHippocampusSpatial BehaviorPharmacologyHippocampusChromatin remodelingEpigenesis GeneticSocial defeatHistone H4Histones03 medical and health sciencesMice0302 clinical medicineRewardCocaineConditioning PsychologicalValproic acidAnimalsEpigeneticsBiological PsychiatryHistone AcetyltransferasesPharmacologySocial stressCerebral CortexbiologyValproic AcidAcetylation030227 psychiatryUp-RegulationHistone Deacetylase InhibitorsDisease Models AnimalHistoneHistone acetylationAcetylationbiology.proteinCentral Nervous System StimulantsPsychologySocial defeat stress030217 neurology & neurosurgeryStress Psychological
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Enzymes involved in the dynamic equilibrium of core histone acetylation ofPhysarum polycephalum

1992

DEAE-Scpharose chromatography of extracts from plasmodia of the myxomyccte PI~.~suru~~t ,~/.~crpl~~ho~~ revealed the presence of multiple histone acetyltransferases and histonc deacctylascs. A cyloplasmic histonc acctyltransferase B, specific for histonc H4, and two nuclear acetyltransferases Al and A2 were identilied; Al acetylates all core hislones with a preference for l-13 and H2A. whereas A2 is specific for H3 and also slightly for H2B. Two hislone deacetylases. HDI and HD2, could be discriminated. They differ with respect to subslralc speciliciiy and pH dependence. For the first time the substrate specificity of histonc deacetylascs was determined using HPLC-purilicd individual core h…

ErythrocytesSaccharomyces cerevisiae ProteinsBiophysicsBiochemistryHistone DeacetylasesSubstrate SpecificityHistonesPhysarumHistone H1AcetyltransferasesPhysarum polycephalumStructural BiologyHistone H2AGeneticsAnimalsHistone deacetylaseHistone octamerMolecular BiologyChromatography High Pressure LiquidHistone AcetyltransferasesHistone AcetyltransferasesbiologyHistone deacetylase 2AcetylationButyrateCell BiologyHistone acetyltransferaseMolecular biologyChromatinHistone Deacetylase InhibitorsIsoenzymesButyratesKineticsHistone acetylationBiochemistryHistone methyltransferasebiology.proteinButyric AcidHistone acetyltransferaseHistone deacetylaseChickensProtein Processing Post-TranslationalFEBS Letters
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Gcn5p is involved in the acetylation of histone H3 in nucleosomes.

1997

Abstract Enzymatic extracts from a gcn5 mutant and wild-type strains of Saccharomyces cerevisiae were chromatographically fractionated and the histone acetyltransferase activities compared. When free histones were used as substrate, extracts from wild-type cells showed two peaks of activity on histone H3 but extracts from gcn5 mutant cells showed only one. With nucleosomes as substrate, the histone acetyltransferase activities present in extracts from the gcn5 mutant strain were not able to modify H3 whereas wild-type cell extracts acetylated intensely this histone. The activity that acetylated nucleosome-bound H3 behaved as a 170-kDa complex. We suggest that Gcn5p represents a catalytic su…

ErythrocytesSaccharomyces cerevisiae ProteinsBiophysicsSaccharomyces cerevisiaeBiochemistryFungal ProteinsHistonesHistone H3Histone H1Structural BiologyHistone H2AHistone methylationGeneticsHistone codeAnimalsHistone octamerMolecular BiologyHistone AcetyltransferasesHistone acetyltransferase GCN5biologyAcetylationCell BiologyHistone acetyltransferaseChromatinNucleosomesDNA-Binding ProteinsMolecular WeightBiochemistryNucleosomeHistone methyltransferasebiology.proteinChickensProtein KinasesFEBS letters
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The Sas3p and Gcn5p histone acetyltransferases are recruited to similar genes.

2006

A macroarray platform was used to identify binding sites of yeast histone acetyltransferase catalytic subunits and to correlate their positions with acetylation of lysine 14 of histone H3, revealing that Sas3p and Gcn5p are recruited to similar sets of intensely transcribed genes.

GeneticsHistone AcetyltransferasesChromatin ImmunoprecipitationSaccharomyces cerevisiae ProteinsResearchAcetylationHistone acetyltransferaseSaccharomyces cerevisiaeSAP30BiologyCell biologyHistonesHistone H3GenòmicaHistone H1Histone methyltransferaseGene Expression Regulation FungalHistone H2Abiology.proteinHistone codeHistone Acetyltransferases
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Interplay among Gcn5, Sch9 and mitochondria during chronological aging of wine yeast is dependent on growth conditions.

2015

Saccharomyces cerevisiae chronological life span (CLS) is determined by a wide variety of environmental and genetic factors. Nutrient limitation without malnutrition, i.e. dietary restriction, expands CLS through the control of nutrient signaling pathways, of which TOR/Sch9 has proven to be the most relevant, particularly under nitrogen deprivation. The use of prototrophic wine yeast allows a better understanding of the role of nitrogen in longevity in natural and more demanding environments, such as grape juice fermentation. We previously showed that acetyltransferase Gcn5, a member of the SAGA complex, has opposite effects on CLS under laboratory and winemaking conditions, and is detrimen…

GrapesSaccharomyces cerevisiae ProteinsNitrogenmedia_common.quotation_subjectSaccharomyces cerevisiaeLongevitylcsh:MedicineWineSaccharomyces cerevisiaeMitochondrionYeastsEndopeptidasesAutophagylcsh:ScienceWinemakingmedia_commonHistone AcetyltransferasesCell NucleusMultidisciplinarybiologyEthanollcsh:RLongevityIntracellular Signaling Peptides and ProteinsNutrientsbiology.organism_classificationYeastMitochondriaSAGA complexYeast in winemakingAutophagic cell deathPhenotypeBiochemistryFermentationFermentationlcsh:QProtein KinasesSignal TransductionTranscription FactorsResearch ArticlePLoS ONE
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Type-II histone deacetylases: elusive plant nuclear signal transducers

2013

Since the beginning of the 21st century, numerous studies have concluded that the plant cell nucleus is one of the cellular compartments that define the specificity of the cellular response to an external stimulus or to a specific developmental stage. To that purpose, the nucleus contains all the enzymatic machinery required to carry out a wide variety of nuclear protein post-translational modifications (PTMs), which play an important role in signal transduction pathways leading to the modulation of specific sets of genes. PTMs include protein (de)acetylation which is controlled by the antagonistic activities of histone acetyltransferases (HATs) and histone deacetylases (HDACs). Regarding p…

Histone AcetyltransferasesGeneticsPhysiologyPlant ScienceBiologyCell biologyHistoneAcetylationbiology.proteinNuclear proteinSignal transductionGeneCellular compartmentProtein deacetylationPlant, Cell & Environment
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