Search results for "Methyltransferases"

showing 8 items of 78 documents

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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Characterization of a novel selenium methyltransferase from freshwater bacteria showing strong similarities with the calicheamicin methyltransferase

2004

A novel group of Se-methyltransferases is presented. The genetic determinant, named mmtA, which revealed this group was isolated from selenite and selenate-resistant freshwater bacteria. E. coli expressing mmtA and grown with a Se supplement emitted dimethyl selenide (DMSe) and dimethyl diselenide (DMDSe). Phylogenetic analysis divided MmtA-like bacterial sequences into two clusters, one grouping MmtA with S- and O-methyltransferases, and one grouping UbiE C-methyltransferases. Se methylation by some of these MmtA phyletic neighbours was investigated.

[SDE] Environmental SciencesMethyltransferaseStereochemistry[SDV]Life Sciences [q-bio]Molecular Sequence DataBiophysicschemistry.chemical_elementBiochemistryGas Chromatography-Mass Spectrometry03 medical and health sciencesStructural BiologyPhylogeneticsGeneticsAmino Acid SequencePeptide sequencePhylogenyComputingMilieux_MISCELLANEOUS030304 developmental biologyDNA Primerschemistry.chemical_classification0303 health sciencesbiologyPhylogenetic treeBacteriaBase SequenceSequence Homology Amino Acid030306 microbiologyMethylationMethyltransferasesbiology.organism_classificationAmino acid[SDV] Life Sciences [q-bio]Biochemistrychemistry[SDE]Environmental SciencesWater MicrobiologyBacteriaSelenium
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Cyclopropane Fatty Acid Synthase from Oenococcus oeni: Expression in Lactococcus lactis subsp. Cremoris and Biochemical Characterization

2015

Bacterial cyclopropane fatty acid synthases (CFA synthases) catalyze the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to the double bond of a lipid chain, thereby forming a cyclopropane ring. CFAs contribute to resistance to acidity, dryness, and osmotic imbalance in many bacteria. This work describes the first biochemical characterization of a lactic acid bacterium CFA synthase. We have overexpressed Oenococcus oeni CFA synthase in E. coli in order to purify the enzyme. The optimum cyclopropanation activity was obtained at pH 5.6 and 35.8 °C. The high K(m) (AdoMet) value obtained (2.26 mM) demonstrates the low affinity of O. oeni enzyme toward the L. lactis subsp. cremo…

[SDV]Life Sciences [q-bio]medicine.disease_causeBiochemistryMicrobiologySubstrate SpecificityMicrobiology03 medical and health scienceschemistry.chemical_compoundEscherichia coliGeneticsmedicineCyclopropane fatty acidMolecular BiologyEscherichia coliOenococcusPhospholipidsComputingMilieux_MISCELLANEOUS030304 developmental biologyOenococcus oenichemistry.chemical_classification0303 health sciences[ SDV ] Life Sciences [q-bio]biologyATP synthase030306 microbiologyLactococcus lactis subsp cremorisFatty AcidsLactococcus lactisGene Expression Regulation BacterialMethyltransferasesGeneral Medicinebiology.organism_classification[SDV] Life Sciences [q-bio]Lactococcus lactisEnzymechemistryBiochemistryMutationbiology.proteinOenococcus
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5-Azacytidine Inhibits the Activation of Senescence Program and Promotes Cytotoxic Autophagy during Trdmt1-Mediated Oxidative Stress Response in Insu…

2022

5-Azacytidine (5-azaC), a methyltransferase inhibitor and anticancer drug, can promote several cellular stress responses such as apoptosis, autophagy, and senescence. The action of 5-azaC is complex and can be modulated by dose, time of treatment, and co-administration with oxidants. Insulinoma is a rare pancreatic neuroendocrine tumor with limited chemotherapeutic options. In the present study, two cellular models of insulinoma were considered, namely NIT-1 and β-TC-6 mouse cells, to evaluate the effects of 5-azaC post-treatment during hydrogen peroxide-induced oxidative stress. 5-azaC attenuated the development of oxidant-induced senescent phenotype in both cell lines. No pro-apoptotic ac…

autophagyAntineoplastic AgentsMethyltransferasesGeneral MedicineinsulinomaOxidantsPancreatic NeoplasmsMiceOxidative Stress5-azacytidinenitric oxideSettore BIO/10 - BiochimicaAzacitidineAnimalsCells
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MiR-221 promotes stemness of breast cancer cells by targeting DNMT3b

2016

// Giuseppina Roscigno 1, 2 , Cristina Quintavalle 1, 2 , Elvira Donnarumma 3 , Ilaria Puoti 1 , Angel Diaz-Lagares 4 , Margherita Iaboni 1 , Danilo Fiore 1 , Valentina Russo 1 , Matilde Todaro 5 , Giulia Romano 6 , Renato Thomas 7 , Giuseppina Cortino 7 , Miriam Gaggianesi 5 , Manel Esteller 4 , Carlo M. Croce 6 , Gerolama Condorelli 1, 2 1 Department of Molecular Medicine and Medical Biotechnology, “Federico II” University of Naples, Naples, Italy 2 IEOS-CNR, Naples, Italy 3 IRCCS-SDN, Naples, Italy 4 Epigenetic and Cancer Biology Program (PEBC) IDIBELL, Hospital Duran I Reynals, Barcelona, Spain 5 Department of Surgical and Oncological Sciences, Cellular and Molecular Pathophysiology Lab…

cancer stem cells0301 basic medicineMicro RNAsCellular differentiationADNDNMTStem cellsStem cell markermedicine.disease_causeBioinformaticsMCF-7 Cell0302 clinical medicineBreast cancerHEK293 CellTumor Cells CulturedDNA (Cytosine-5-)-MethyltransferasesOligonucleotide Array Sequence AnalysisMicroscopy ConfocalReverse Transcriptase Polymerase Chain ReactionMicroRNAHomeodomain ProteinNanog Homeobox ProteinmicroRNAsGene Expression Regulation NeoplasticOncology030220 oncology & carcinogenesisMCF-7 CellsNeoplastic Stem CellsRNA InterferenceCèl·lules mareBreast NeoplasmResearch PaperHumanHomeobox protein NANOGBlotting WesternBreast NeoplasmsBiologyCàncer de mama03 medical and health sciencesmicroRNAs breast cancer cancer stem cells DNMTBreast cancerCancer stem cellCell Line TumorSpheroids CellularmedicineHumansHomeodomain ProteinsOligonucleotide Array Sequence AnalysiCancer stem cellGene Expression ProfilingCancerDNAmedicine.diseaseMolecular medicineMicroRNAsHEK293 Cells030104 developmental biologyDNA (Cytosine-5-)-MethyltransferaseCancer researchNeoplastic Stem CellCarcinogenesisOctamer Transcription Factor-3
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Estradiol, acting through estrogen receptor alpha, restores dimethylarginine dimethylaminohydrolase activity and nitric oxide production in oxLDL-tre…

2011

Asymmetric dimethylarginine (ADMA) is an endogenous inhibitor of nitric oxide (NO) synthase. ADMA accumulation, mainly due to a decreased dimethylarginine dimethylaminohydrolase (DDAH) activity, has been related to the development of cardiovascular diseases. We investigate whether estradiol prevents the changes induced by oxidized low density lipoprotein (oxLDL) on the DDAH/ADMA/NO pathway in human umbilical artery endothelial cells (HUAEC). HUAEC were exposed to estradiol, native LDL (nLDL), oxLDL and their combinations for 24 h. In some experiments, cells were also exposed to the unspecific estrogen receptor (ER) antagonist ICI 182780, the specific ERα antagonist MPP or specific agonists …

medicine.medical_specialtyProtein-Arginine N-MethyltransferasesEndotheliumNitric Oxide Synthase Type IIImedicine.drug_classBlotting WesternArginineNitric OxideBiochemistryUmbilical ArteriesNitric oxideAmidohydrolasesReceptors G-Protein-Coupledchemistry.chemical_compoundEndocrinologyEnosInternal medicinemedicineEstrogen Receptor betaHumansEstrogens Non-SteroidalMolecular BiologyCells CulturedbiologyEstradiolArtèriesProtein StabilityEstrogen AntagonistsEstrogen Receptor alphaEndoteli vascularbiology.organism_classificationNitric oxide synthaseIsoenzymesLipoproteins LDLRepressor Proteinsmedicine.anatomical_structureEndocrinologychemistryReceptors EstrogenEstrogenbiology.proteinlipids (amino acids peptides and proteins)Endothelium VascularAsymmetric dimethylarginineEstrogen receptor alphaGPER
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Functional characterization of the human tRNA methyltransferases TRMT10A and TRMT10B

2020

Abstract The TRM10 family of methyltransferases is responsible for the N1-methylation of purines at position 9 of tRNAs in Archaea and Eukarya. The human genome encodes three TRM10-type enzymes, of which only the mitochondrial TRMT10C was previously characterized in detail, whereas the functional significance of the two presumably nuclear enzymes TRMT10A and TRMT10B remained unexplained. Here we show that TRMT10A is m1G9-specific and methylates a subset of nuclear-encoded tRNAs, whilst TRMT10B is the first m1A9-specific tRNA methyltransferase found in eukaryotes and is responsible for the modification of a single nuclear-encoded tRNA. Furthermore, we show that the lack of G9 methylation cau…

tRNA MethyltransferasesMethyltransferaseBase SequenceAcademicSubjects/SCI00010Nucleic Acid EnzymesTRNA MethyltransferaseRNAMethylationMethyltransferasesMitochondrionBiologyMethylationTRNA MethyltransferasesCell LineBiochemistryRNA TransferPurinesProtein BiosynthesisTransfer RNAProtein biosynthesisGeneticsHumans
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Eukaryotic rRNA Modification by Yeast 5-Methylcytosine-Methyltransferases and Human Proliferation-Associated Antigen p120.

2015

International audience; Modified nucleotide 5-methylcytosine (m(5)C) is frequently present in various eukaryotic RNAs, including tRNAs, rRNAs and in other non-coding RNAs, as well as in mRNAs. RNA: m(5)C-methyltranferases (MTases) Nop2 from S. cerevisiae and human proliferation-associated nucleolar antigen p120 are both members of a protein family called Nop2/NSUN/NOL1. Protein p120 is well-known as a tumor marker which is over-expressed in various cancer tissues. Using a combination of RNA bisulfite sequencing and HPLC-MS/MS analysis, we demonstrated here that p120 displays an RNA:m(5)C-MTase activity, which restores m(5)C formation at position 2870 in domain V of 25S rRNA in a nop2 Delta …

tRNA MethyltransferasesSaccharomyces cerevisiae Proteinslcsh:RNuclear Proteinslcsh:MedicineMethyltransferasesSaccharomyces cerevisiaeProtein Structure TertiaryRNA Ribosomal5-MethylcytosineHumans[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biologylcsh:Qlcsh:Science[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyProtein BindingResearch ArticlePLoS ONE
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