Search results for "histone acetyltransferase"

showing 10 items of 50 documents

Role of Redox Signaling, Protein Phosphatases and Histone Acetylation in the Inflammatory Cascade in Acute Pancreatitis: Therapeutic Implications

2010

Acute pancreatitis starts as a local inflammation of the pancreatic tissue but often leads to the systemic inflammatory response syndrome and death by multiple organ failure. Pro-inflammatory cytokines, particularly TNF-alpha and Il-1beta, play a pivotal role together with oxidative stress and glutathione depletion in the inflammatory response in this disease. Most inflammatory mediators act through mitogen activated protein kinases and nuclear factor kB. Nevertheless, elucidation of the precise mechanisms involved in activation and attenuation phases of the inflammatory cascade is still underway. Redox signaling mediated by inactivation of protein phosphatases and histone acetylation trigg…

Phosphodiesterase InhibitorsImmunologyPhosphataseBiologyHistonesDual-specificity phosphatasePhosphoprotein PhosphatasesHumansImmunology and AllergyPancreasHistone AcetyltransferasesInflammationPharmacologyHistone AcetyltransferasesKinaseAcetylationGeneral MedicineProtein phosphatase 2ChromatinCell biologyHistone Deacetylase InhibitorsHistonePancreatitisBiochemistryAcetylationAcute Diseasebiology.proteinSignal transductionOxidation-ReductionSignal TransductionInflammation & Allergy - Drug Targets
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Regulation of NADPH oxidase-mediated superoxide production by acetylation and deacetylation

2021

Oral treatment of apolipoprotein E-knockout (ApoE-KO) mice with the putative sirtuin 1 (SIRT1) activator resveratrol led to a reduction of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase activity in the heart. In contrast, the SIRT1 inhibitor EX527 enhanced the superoxide production in isolated human polymorphonuclear granulocytes. In human monocytic THP-1 cells, phorbol ester-stimulated superoxide production was enhanced by inhibitors of histone deacetylases (HDACs; including quisinostat, trichostatin A (TSA), PCI34051, and tubastatin A) and decreased by inhibitors of histone acetyltransferases [such as garcinol, curcumin, and histone acetyltransferase (HAT) Inhibitor II]. Thes…

Physiologyresveratrolsirtuin 1histone acetyltransferaseSirtuinechemistry.chemical_compoundHistone deacetylasesSirtuin 1Physiology (medical)NADPH-OxidasemedicineQP1-981ddc:610Original ResearchacetylationAcetyltransferasenNADPH oxidasebiologyNADPH oxidaseSirtuin 1SuperoxideAcetylationHistone acetyltransferaseTrichostatin AchemistryBiochemistryHistone acetyltransferasesAcetylationResveratrolNADPH oxidaseshistone deacetylasebiology.proteinHistone deacetylaseDDC 610 / Medicine & healthNicotinamide adenine dinucleotide phosphateRac1medicine.drug
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Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast.

2014

Elongator is a conserved protein complex comprising six different polypeptides that has been ascribed a wide range of functions, but which is now known to be required for modification of uridine residues in the wobble position of a subset of tRNAs in yeast, plants, worms and mammals. In previous work, we showed that Elongator's largest subunit (Elp1; also known as Iki3) was phosphorylated and implicated the yeast casein kinase I Hrr25 in Elongator function. Here we report identification of nine in vivo phosphorylation sites within Elp1 and show that four of these, clustered close to the Elp1 C-terminus and adjacent to a region that binds tRNA, are important for Elongator's tRNA modification…

ProteomicsSaccharomyces cerevisiae Proteinslcsh:QH426-470Saccharomyces cerevisiaeBiochemistryMolecular GeneticsRNA TransferGene Expression Regulation FungalMolecular Cell BiologyGeneticsFungal GeneticsPhosphorylationPost-Translational ModificationUridineMolecular BiologyAdaptor Proteins Signal TransducingHistone AcetyltransferasesAlanineSpectrometric Identification of ProteinsBiology and life sciencesCasein Kinase INucleotidesMicrobial GeneticsProteinsCell BiologyPeptide Elongation Factorslcsh:GeneticsPhenotypeMultiprotein ComplexesRNAMolecular ComplexesTransfer RNAAnticodonsResearch ArticlePLoS genetics
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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
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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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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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Bromodomain factor 1 (Bdf1) protein interacts with histones

2001

AbstractUsing a yeast two-hybrid assay we detected an interaction between the N-terminal region of histone H4 (amino acids 1–59) and a fragment of the bromodomain factor 1 protein (Bdf1p) (amino acids 304–571) that includes one of the two bromodomains of this protein. No interaction was observed using fragments of histone H4 sequence smaller than the first 59 amino acids. Recombinant Bdf1p (rBdf1p) demonstrates binding affinity for histones H4 and H3 but not H2A and H2B in vitro. Moreover, rBdf1p is able to bind histones H3 and H4 having different degrees of acetylation. Finally, we have not detected histone acetyltransferase activity associated with Bdf1p.

Saccharomyces cerevisiae ProteinsRecombinant Fusion ProteinsBiophysicsBromodomainTwo-hybridBiochemistryFungal ProteinsHistonesHistone H4SaccharomycesAcetyltransferasesGenes ReporterStructural BiologyTwo-Hybrid System TechniquesHistone methylationHistone H2AGeneticsHistone acetyltransferase activityHistone octamerMolecular BiologyHistone AcetyltransferasesBromodomain factor 1 proteinbiologyChemistryCell BiologyHistone acetyltransferasePeptide FragmentsChromatinBromodomainHistoneBiochemistryPCAFbiology.proteinHistone acetyltransferaseProtein BindingTranscription FactorsFEBS Letters
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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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AcetyltransferaseSAS2and sirtuinSIR2,respectively, control flocculation and biofilm formation in wine yeast

2014

Cell-to-cell and cell-to-environment interactions of microorganisms are of substantial relevance for their biotechnological use. In the yeast Saccharomyces cerevisiae, flocculation can be an advantage to clarify final liquid products after fermentation, and biofilm formation may be relevant for the encapsulation of strains of interest. The adhesion properties of wine yeast strains can be modified by the genetic manipulation of transcriptional regulatory proteins, such as histone deacetylases, and acetylases. Sirtuin SIR2 is essential for the formation of mat structures, a kind of biofilm that requires the expression of cell-wall protein FLO11 as its deletion reduces FLO11 expression, and ad…

Saccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeWineSaccharomyces cerevisiaeApplied Microbiology and BiotechnologyMicrobiologySirtuin 2Gene Expression Regulation FungalAllelesSilent Information Regulator Proteins Saccharomyces cerevisiaeHistone AcetyltransferasesWinebiologyBiofilmFlocculationfood and beveragesGeneral Medicinebiology.organism_classificationYeastYeast in winemakingPhenotypeBiochemistryBiofilmsAcetyltransferaseFermentationSirtuinbiology.proteinFermentationGene DeletionFEMS Yeast Research
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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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