Search results for "histone methylation"

showing 6 items of 36 documents

Functional antagonism between histone H3K4 demethylases in vivo

2011

Dynamic regulation of histone modifications is critical during development, and aberrant activity of chromatin-modifying enzymes has been associated with diseases such as cancer. Histone demethylases have been shown to play a key role in eukaryotic gene transcription; however, little is known about how their activities are coordinated in vivo to regulate specific biological processes. In Drosophila, two enzymes, dLsd1 (Drosophila ortholog of lysine-specific demethylase 1) and Lid (little imaginal discs), demethylate histone H3 at Lys 4 (H3K4), a residue whose methylation is associated with actively transcribed genes. Our studies show that compound mutation of Lid and dLsd1 results in increa…

Settore BIO/11 - Biologia MolecolareBiologyMethylationHistoneshistone demethylasesHistone H3HeterochromatinHistone H2AHistone methylationGeneticsAnimalsDrosophila ProteinsHistone codeGeneticsReceptors NotchEZH2Oxidoreductases N-DemethylatingHistone-Lysine N-MethyltransferaseSettore BIO/18 - GeneticaDrosophila melanogasterPhenotypeGene Expression RegulationHistone methyltransferaseMutationHeterochromatin protein 1Histone DemethylasesSignal TransductionResearch PaperDevelopmental Biology
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Epigenetic Regulation of Early- and Late-Response Genes in Acute Pancreatitis

2015

Abstract Chromatin remodeling seems to regulate the patterns of proinflammatory genes. Our aim was to provide new insights into the epigenetic mechanisms that control transcriptional activation of early- and late-response genes in initiation and development of severe acute pancreatitis as a model of acute inflammation. Chromatin changes were studied by chromatin immunoprecipitation analysis, nucleosome positioning, and determination of histone modifications in promoters of proinflammatory genes in vivo in the course of taurocholate-induced necrotizing pancreatitis in rats and in vitro in rat pancreatic AR42J acinar cells stimulated with taurocholate or TNF-α. Here we show that the upregulat…

Taurocholic AcidTranscriptional Activation0301 basic medicineChromatin ImmunoprecipitationImmunologyAcinar CellsBiologyMethylationChromatin remodelingEpigenesis GeneticHistones03 medical and health sciences0302 clinical medicineHistone methylationAnimalsImmunology and AllergyNucleosomeEpigeneticsPromoter Regions GeneticEarly Growth Response Protein 1Histone AcetyltransferasesInflammationPancreatitis Acute NecrotizingTumor Necrosis Factor-alphaDNA HelicasesNuclear ProteinsAcetylationHistone acetyltransferaseChromatin Assembly and DisassemblyRatsChromatin030104 developmental biologyHistoneGene Expression Regulation030220 oncology & carcinogenesisbiology.proteinCancer researchProtein Processing Post-TranslationalChromatin immunoprecipitationTranscription FactorsThe Journal of Immunology
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The histone deacetylase Rpd3 regulates the heterochromatin structure of Drosophila telomeres

2011

Telomeres are specialized structures at the end of eukaryotic chromosomes that are required to preserve genome integrity, chromosome stability and nuclear architecture. Telomere maintenance and function are established epigenetically in several eukaryotes. However, the exact chromatin enzymatic modifications regulating telomere homeostasis are poorly understood. In Drosophila melanogaster, telomere length and stability are maintained through the retrotransposition of specialized telomeric sequences and by the specific loading of protecting capping proteins, respectively. Here, we show that the loss of the essential and evolutionarily conserved histone deacetylase Rpd3, the homolog of mammal…

Telomere-binding proteinGeneticsEpigenomicsMaleHistone deacetylase 5Histone deacetylase 2HDAC11Histone Deacetylase 1Cell BiologyBiologyTelomereHistone H4Telomere HomeostasisDrosophila melanogasterHeterochromatinHistone H2Ahistone deacetylaseHistone codeAnimalsDrosophila Proteinsanimals; article; chromosome aberration; chromosome structure; drosophila; drosophila melanogaster; drosophila proteins; enzyme activity; epigenetics; epigenomics; eukaryota; heterochromatin; histone acetylation; histone deacetylase 1; histone deacetylase rpd 3; histone methylation; male; mammalia; nonhuman; polytene chromosome; priority journal; regulatory mechanism; telomere; unclassified drugPolytene Chromosomes
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Nucleosome-specific, Time-dependent Changes in Histone Modifications during Activation of the Early Growth Response 1 (Egr1) Gene

2014

Histone post-translational modifications and nucleosome remodeling are coordinate events involved in eukaryotic transcriptional regulation. There are relatively few data on the time course with which these events occur in individual nucleosomes. As a contribution to fill this gap, we first describe the nature and time course of structural changes in the nucleosomes -2, -1, and +1 of the murine Egr1 gene upon induction. To initiate the transient activation of the gene, we used the stimulation of MLP29 cells with phorbol esters and the in vivo activation after partial hepatectomy. In both models, nucleosomes -1 and +1 are partially evicted, whereas nucleosomes +1 and -2 slide downstream durin…

Time FactorsTranscription GeneticBiologyBiochemistryChromatin remodelingCell LineHistonesMiceHistone H1Histone methylationAnimalsHepatectomyHistone codeNucleosomeGene RegulationPromoter Regions GeneticMolecular BiologyEarly Growth Response Protein 1Mice KnockoutCell BiologyMolecular biologySWI/SNFLiver RegenerationNucleosomesCell biologyHistoneLiverChromatosomeHepatocytesbiology.proteinTetradecanoylphorbol AcetateProtein Processing Post-TranslationalJournal of Biological Chemistry
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Dynamic remodeling of histone modifications in response to osmotic stress in Saccharomyces cerevisiae.

2014

Abstract Background Specific histone modifications play important roles in chromatin functions; i.e., activation or repression of gene transcription. This participation must occur as a dynamic process. Nevertheless, most of the histone modification maps reported to date provide only static pictures that link certain modifications with active or silenced states. This study, however, focuses on the global histone modification variation that occurs in response to the transcriptional reprogramming produced by a physiological perturbation in yeast. Results We did a genome-wide chromatin immunoprecipitation analysis for eight specific histone modifications before and after saline stress. The most…

Transcriptional ActivationOsmotic stressTranscription GeneticSaccharomyces cerevisiaeBiologyMethylationChromatin remodelingHistonesOsmotic PressureStress PhysiologicalGene Expression Regulation FungalHistone methylationGeneticsHistone codeRNA MessengerGenome-wideChIP-ChipRegulation of gene expressionAcetylationChromatin Assembly and DisassemblyMolecular biologyChromatinChromatinCell biologyGene regulationHistoneAcetylationMultigene Familybiology.proteinEpigeneticsRNA Polymerase IIGenome FungalHistone modificationChromatin immunoprecipitationTranscriptionBiotechnologyResearch ArticleBMC genomics
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The Histone Acetyl-Transferase MOZ Cooperates with the Histone Methyl-Transferase MLL to Regulate HOX Gene Expression in Human Hematopoietic Stem Cel…

2008

Abstract MOZ (MOnocytic leukaemia Zinc finger protein) (also called MYST3 or KAT6A) is a member of the MYST family of HATs which likely acetylate H4K16. The MLL (MixedLineageLeukemia) gene is a frequent target for recurrent chromosomal translocations found in AML and ALL. MLL (KMT2A) is a methyl-transferase targeting H3K4. It was shown that MOZ/CBP leukemia, as observed in MLL-rearranged leukemias, harbors abnormal levels of homeobox (HOX) genes expression. HOX transcription factors have a crucial function in hematopoiesis regulation. In addition, HOXA5, HOXA7, and HOXA9 are often considered to be pivotal HOX genes for MLL transformation, constituting downstream targets of MLL. In our study…

biologyImmunologyCell BiologyHematologyBiochemistryMYST3Molecular biologyHistone H3Histonehemic and lymphatic diseasesHistone methyltransferaseHistone methylationbiology.proteinH3K4me3WDR5Hox geneneoplasmsBlood
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