Search results for "Histone-Lysine N-Methyltransferase"

showing 9 items of 29 documents

FSHD muscular dystrophy region gene 1 binds Suv4-20h1 histone methyltransferase and impairs myogenesis.

2013

Facioscapulohumeral muscular dystrophy (FSHD) is an autosomal dominant myopathy with a strong epigenetic component. It is associated with deletion of a macrosatellite repeat leading to over-expression of the nearby genes. Among them, we focused on FSHD region gene 1 (FRG1) since its over-expression in mice, Xenopus laevis and Caenorhabditis elegans, leads to muscular dystrophy-like defects, suggesting that FRG1 plays a relevant role in muscle biology. Here we show that, when over-expressed, FRG1 binds and interferes with the activity of the histone methyltransferase Suv4-20h1 both in mammals and Drosophila. Accordingly, FRG1 over-expression or Suv4-20h1 knockdown inhibits myogenesis. Moreov…

Muscle DevelopmentEvolution Molecular03 medical and health sciencesMice0302 clinical medicineGeneticsmedicineFacioscapulohumeral muscular dystrophyMyocyteAnimalsHumansEpigeneticsMuscular dystrophyMyopathyMolecular Biology030304 developmental biologyCell NucleusMice Knockout0303 health sciencesMuscle CellsbiologyMyogenesisMicrofilament ProteinsNuclear ProteinsProteinsRNA-Binding ProteinsCell DifferentiationCell BiologyGeneral MedicineHistone-Lysine N-MethyltransferaseMuscular Dystrophy Animalmedicine.diseaseMolecular biologyHistoneDrosophila melanogasterHEK293 CellsPhenotypeOrgan SpecificityHistone methyltransferaseEpigenetic deregulation by FRG1Gene Knockdown Techniquesbiology.proteinmedicine.symptomCarrier Proteins030217 neurology & neurosurgeryProtein BindingJournal of molecular cell biology
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Synergistic targeting of FLT3 mutations in AML via combined menin-MLL and FLT3 inhibition

2020

Abstract The interaction of menin (MEN1) and MLL (MLL1, KMT2A) is a dependency and provides a potential opportunity for treatment of NPM1-mutant (NPM1mut) and MLL-rearranged (MLL-r) leukemias. Concomitant activating driver mutations in the gene encoding the tyrosine kinase FLT3 occur in both leukemias and are particularly common in the NPM1mut subtype. In this study, transcriptional profiling after pharmacological inhibition of the menin-MLL complex revealed specific changes in gene expression, with downregulation of the MEIS1 transcription factor and its transcriptional target gene FLT3 being the most pronounced. Combining menin-MLL inhibition with specific small-molecule kinase inhibitors…

NPM1Transcription GeneticImmunologyApoptosisBiochemistryMiceRandom AllocationMice Inbred NODCell Line TumorProto-Oncogene Proteinshemic and lymphatic diseasesAntineoplastic Combined Chemotherapy ProtocolsGene expressionmedicineAnimalsHumansMEN1PhosphorylationMyeloid Ecotropic Viral Integration Site 1 ProteinProtein Kinase InhibitorsneoplasmsbiologyGene Expression Regulation LeukemicKinaseNuclear ProteinsMyeloid leukemiaDrug SynergismHistone-Lysine N-MethyltransferaseCell BiologyHematologymedicine.diseaseCoculture TechniquesNeoplasm ProteinsLeukemia Myeloid AcuteLeukemiaKMT2Afms-Like Tyrosine Kinase 3biology.proteinCancer researchNucleophosminProtein Processing Post-TranslationalTyrosine kinaseMyeloid-Lymphoid Leukemia ProteinBlood
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Establishment of Polycomb silencing requires a transient interaction between PC and ESC

2001

Two distinct types of Polycomb complexes have been identified in flies and in vertebrates, one containing ESC and one containing PC. Using LexA fusions, we show that PC and ESC can establish silencing of a reporter gene but that each requires the presence of the other. In early embryonic extracts, we find PC transiently associated with ESC in a complex that includes EZ, PHO, PH, GAGA, and RPD3 but not PSC. In older embryos, PC is found in a complex including PH, PSC, GAGA, and RPD3, whereas ESC is in a separate complex including EZ, PHO, and RPD3.

Polycomb-Group ProteinsRepressorSettore BIO/11 - Biologia MolecolarePlasma protein bindingBiologyPolycomb silencingResearch CommunicationGeneticsPolycomb-group proteinsAnimalsDrosophila ProteinsGene silencingGene Silencingreproductive and urinary physiologyPolycomb Repressive Complex 1Reporter geneurogenital systemPolycomb Repressive Complex 2PcG complexEmbryoHistone-Lysine N-MethyltransferasePrecipitin TestsEmbryonic stem cellMolecular biologyRepressor Proteinsembryonic structuresInsect ProteinsDrosophilaRepressor lexAbiological phenomena cell phenomena and immunityESC/PHOProtein BindingDevelopmental BiologyGenes & Development
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Excess of de novo variants in genes involved in chromatin remodelling in patients with marfanoid habitus and intellectual disability.

2020

PurposeMarfanoid habitus (MH) combined with intellectual disability (ID) (MHID) is a clinically and genetically heterogeneous presentation. The combination of array CGH and targeted sequencing of genes responsible for Marfan or Lujan–Fryns syndrome explain no more than 20% of subjects.MethodsTo further decipher the genetic basis of MHID, we performed exome sequencing on a combination of trio-based (33 subjects) or single probands (31 subjects), of which 61 were sporadic.ResultsWe identified eight genes with de novo variants (DNVs) in at least two unrelated individuals (ARID1B, ATP1A1, DLG4, EHMT1, NFIX, NSD1, NUP205 and ZEB2). Using simulation models, we showed that five genes (DLG4, NFIX, …

ProbandMale[SDV]Life Sciences [q-bio]intellectual deficiencyMESH: NFI Transcription Factorschromatin remodelingMarfan SyndromeCraniofacial AbnormalitiesMESH: ChildIntellectual disabilityMESH: Craniofacial AbnormalitiesMESH: Mental Retardation X-LinkedExomeChildde novo variantsGenetics (clinical)Exome sequencingGeneticsMESH: ExomeMESH: Middle AgedbiologyMESH: Genetic Predisposition to DiseaseMiddle AgedNFIXMESH: Young AdultFemaleAdultMESH: MutationAdolescentChromatin remodelingMESH: Intellectual DisabilityMESH: Marfan SyndromeEHMT1Young AdultMESH: Whole Exome SequencingIntellectual DisabilityExome SequencingGeneticsmedicineHumansGenetic Predisposition to Diseasemarfanoid habitusGeneMESH: Neurodevelopmental DisordersMESH: AdolescentMESH: HumansGenetic heterogeneityMESH: Chromatin Assembly and DisassemblyMESH: Histone-Lysine N-MethyltransferaseMESH: AdultHistone-Lysine N-Methyltransferasemedicine.diseaseChromatin Assembly and DisassemblyMESH: MaleNFI Transcription FactorsNeurodevelopmental DisordersMutationbiology.proteinMental Retardation X-LinkedMESH: FemaleJournal of medical genetics
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Protein Interactions within the Set1 Complex and Their Roles in the Regulation of Histone 3 Lysine 4 Methylation

2006

Set1 is the catalytic subunit and the central component of the evolutionarily conserved Set1 complex (Set1C) that methylates histone 3 lysine 4 (H3K4). Here we have determined protein/protein interactions within the complex and related the substructure to function. The loss of individual Set1C subunits differentially affects Set1 stability, complex integrity, global H3K4 methylation, and distribution of H3K4 methylation along active genes. The complex requires Set1, Swd1, and Swd3 for integrity, and Set1 amount is greatly reduced in the absence of the Swd1-Swd3 heterodimer. Bre2 and Sdc1 also form a heteromeric subunit, which requires the SET domain for interaction with the complex, and Sdc…

Saccharomyces cerevisiae ProteinsProtein subunitLysineRNA polymerase IISaccharomyces cerevisiaeMethylationenvironment and public healthBiochemistryProtein–protein interactionHistonesSerineGene Expression Regulation FungalCoding regionMolecular BiologybiologyLysineHistone-Lysine N-MethyltransferaseCell BiologyMethylationDNA-Binding ProteinsProtein SubunitsHistoneBiochemistrybiology.proteinProtein BindingTranscription FactorsJournal of Biological Chemistry
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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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Retrotransposon silencing and telomere integrity in somatic cells of Drosophila depends on the cytosine-5 methyltransferase DNMT2

2009

Here we show that the cytosine-5 methyltransferase DNMT2 controls retrotransposon silencing in Drosophila somatic cells. In Drosophila, significant DNMT2-dependent DNA methylation occurs during early embryogenesis. Suppression of white gene silencing by Mt2 (Dnmt2) null mutations in variegated P[w(+)] element insertions identified functional targets of DNMT2. The enzyme controls DNA methylation at retrotransposons in early embryos and initiates histone H4K20 trimethylation catalyzed by the SUV4-20 methyltransferase. In somatic cells, loss of DNMT2 eliminates H4K20 trimethylation at retrotransposons and impairs maintenance of retrotransposon silencing. In Dnmt2 and Suv4-20 null genotypes, re…

Transposable elementDNA-Cytosine MethylasesEmbryo NonmammalianMethyltransferaseRetroelementsSomatic cellRetrotransposonGene Knockout TechniquesDrosophilidaeGeneticsAnimalsDrosophila ProteinsGene silencingDNA (Cytosine-5-)-MethyltransferasesGene SilencingCrosses GeneticIn Situ Hybridization FluorescenceGeneticsbiologyfungifood and beveragesHistone-Lysine N-MethyltransferaseDNA MethylationTelomerebiology.organism_classificationTelomereMutationDrosophilaDrosophila melanogasterNature Genetics
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Higher plants possess two different types of ATX1-like copper chaperones.

2007

Abstract Copper (Cu) chaperones constitute a family of small Cu+-binding proteins required for Cu homeostasis in eukaryotes. The ATX1 family of Cu chaperones specifically delivers Cu to heavy metal P-type ATPases. The plant Arabidopsis thaliana expresses the ATX1-like Cu chaperone CCH, which exhibits a plant-specific carboxy-terminal domain (CTD) with unique structural properties. We show that CCH homologues from other higher plants contain CTDs with structural properties similar to Arabidopsis CCH. Furthermore, we identify a new ATX1-like Cu chaperone in Arabidopsis, AtATX1, which functionally complements yeast atx1Δ and sod1Δ associated phenotypes, and localizes to the cytosol of Arabidop…

endocrine systemATPaseTwo-hybrid screeningBiophysicsArabidopsischemistry.chemical_elementBiochemistryArabidopsisMolecular BiologyAdenosine TriphosphatasesbiologyArabidopsis ProteinsCell BiologyHistone-Lysine N-Methyltransferasebiology.organism_classificationPhenotypeCopperYeastProtein Structure TertiaryCytosolBiochemistrychemistryChaperone (protein)biology.proteinCopperGenome PlantMolecular ChaperonesTranscription FactorsBiochemical and biophysical research communications
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Epigenetic siRNA and Chemical Screens Identify SETD8 Inhibition as a Therapeutic Strategy for p53 Activation in High-Risk Neuroblastoma

2017

Given the paucity of druggable mutations in high-risk neuroblastoma (NB), we undertook chromatin-focused small interfering RNA and chemical screens to uncover epigenetic regulators critical for the differentiation block in high-risk NB. High-content Opera imaging identified 53 genes whose loss of expression led to a decrease in NB cell proliferation and 16 also induced differentiation. From these, the secondary chemical screen identified SETD8, the H4K20me1 methyltransferase, as a druggable NB target. Functional studies revealed that SETD8 ablation rescued the pro-apoptotic and cell-cycle arrest functions of p53 by decreasing p53K382me1, leading to activation of the p53 canonical pathway. I…

p530301 basic medicineCancer ResearchSmall interfering RNAMethyltransferaseCellular differentiationDruggabilityBiologyArticleEpigenesis GeneticNeuroblastoma03 medical and health sciences0302 clinical medicineNeuroblastomamedicineHumansEpigeneticsRNA Small InterferingGeneCell ProliferationsiRNA screenCell growthQuinazolineCell DifferentiationdifferentiationHistone-Lysine N-Methyltransferasemedicine.diseaseSETD8030104 developmental biologyOncology030220 oncology & carcinogenesisQuinazolinesCancer researchdifferentiation; epigenetics; neuroblastoma; p53; SETD8; siRNA screen; Oncology; Cell Biology; Cancer ResearchTumor Suppressor Protein p53epigeneticHuman
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