Search results for "ACETYLATION"

showing 10 items of 140 documents

Telomerase and Telomere Length in Pulmonary Fibrosis

2013

In addition to its expression in stem cells and many cancers, telomerase activity is transiently induced in murine bleomycin (BLM)-induced pulmonary fibrosis with increased levels of telomerase transcriptase (TERT) expression, which is essential for fibrosis. To extend these observations to human chronic fibrotic lung disease, we investigated the expression of telomerase activity in lung fibroblasts from patients with interstitial lung diseases (ILDs), including idiopathic pulmonary fibrosis (IPF). The results showed that telomerase activity was induced in more than 66% of IPF lung fibroblast samples, in comparison with less than 29% from control samples, some of which were obtained from lu…

Pulmonary and Respiratory MedicineMaleTelomerasePathologymedicine.medical_specialtyClinical BiochemistryBiologyBleomycinGene Expression Regulation EnzymologicHistonesTelomerase RNA componentIdiopathic pulmonary fibrosischemistry.chemical_compoundBleomycinMiceFibrosisPulmonary fibrosismedicineAnimalsHumansEmfisema pulmonarPromoter Regions GeneticMolecular BiologyLungTelomeraseCells CulturedMice KnockoutLungAntibiotics AntineoplasticAcetylationCell BiologyArticlesFibroblastsTelomererespiratory systemmedicine.diseaseIdiopathic Pulmonary FibrosisTelomereUp-Regulationrespiratory tract diseasesmedicine.anatomical_structurechemistryPulmonsChronic DiseaseCancer researchFemaleAlveolitis Extrinsic AllergicPulmons Malalties
researchProduct

Cyclic AMP-induced Chromatin Changes Support the NFATc-mediated Recruitment of GATA-3 to the Interleukin 5 Promoter

2008

Elevated intracellular cyclic AMP levels, which suppress the proliferation of naive T cells and type 1 T helper (Th1) cells are a property of T helper 2 (Th2) cells and regulatory T cells. While cyclic AMP signals interfere with the IL-2 promoter induction, they support the induction of Th2-type genes, in particular of il-5 gene. We show here that cyclic AMP signals support the generation of three inducible DNase I hypersensitive chromatin sites over the il-5 locus, including its promoter region. In addition, cyclic AMP signals enhance histone H3 acetylation at the IL-5 promoter and the concerted binding of GATA-3 and NFATc to the promoter. This is facilitated by direct protein-protein inte…

Quantitative Trait LociGATA3 Transcription FactorBiologyBiochemistryCell LineHistonesMiceTh2 CellsCyclic AMPTranscriptional regulationAnimalsHumansTranscription Chromatin and EpigeneticsPromoter Regions GeneticHistone H3 acetylationMolecular BiologyInterleukin 5Cell ProliferationMice Inbred BALB CNFATC Transcription FactorsEffectorLymphokineAcetylationZinc FingersPromoterCell BiologyDNA-binding domainTh1 CellsChromatin Assembly and DisassemblyMolecular biologyChromatinProtein Structure TertiaryChromatinGene Expression RegulationInterleukin-2Interleukin-5Signal TransductionJournal of Biological Chemistry
researchProduct

Enzyme-catalysed transformations of ent-kaurane diterpenoids

2005

Several acetyl derivatives of linearol, atractyligenin and atractylitriol were obtained through enzyme-catalysed acetylation and deacetylation reactions. In most reactions lipases showed regio- and stereoselective behaviour, allowing a family of novel compounds to be prepared. Fil: Monsalve, Leandro Nicolas. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Unidad de Microanálisis y Métodos Físicos en Química Orgánica. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Unidad de Microanálisis y Métodos Físicos en Química Orgánica; Argentina. Universidad de Buenos Aires. Facultad de Ciencias Exactas y …

Química OrgánicaACETYLATIONENZYME CATALYSISChemistryStereochemistryDEACETYLATIONOrganic ChemistryENT-KAURANESCiencias QuímicasDITERPENOIDSPhysical and Theoretical ChemistryEnt kauraneCIENCIAS NATURALES Y EXACTAS
researchProduct

Yeast contains multiple forms of histone acetyltransferase.

1989

We have assayed several methods to quantitatively recover yeast histone acetyltransferases in an attempt to study the multiplicity of enzymatic activities. Two methods, namely (NH4)2SO4 precipitation and salt dissociation of chromatin in 0.5 M NaCl, yielded convenient preparations of total histone acetyltransferases. DEAE-Sepharose chromatography of the crude extracts resulted in the separation of three peaks of activity when total yeast histones were used as substrate. However, the scanning of the enzymatic activity toward individual histones along the chromatography, achieved by determining the specific activity of the individual histones after incubating whole histones and [14C]acetyl-Co…

Saccharomyces cerevisiae ProteinsIon chromatographySaccharomyces cerevisiaeBiochemistryHistone DeacetylasesSubstrate SpecificityHistonesAcetyltransferasesEnzyme StabilityHistone octamerMolecular BiologyHistone AcetyltransferasesHistone AcetyltransferasesChromatographybiologyChemistryAcetylationCell BiologyHistone acetyltransferaseChromatography Ion ExchangeYeastChromatinChromatinIsoenzymesKineticsHistoneBiochemistryAcetylationbiology.proteinThe Journal of biological chemistry
researchProduct

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
researchProduct

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
researchProduct

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
researchProduct

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
researchProduct

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
researchProduct

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
researchProduct