Search results for " methylation"

showing 10 items of 457 documents

Mutation rate of bacteriophage ΦX174 modified through changes in GATC sequence context

2011

Bacteriophage ΦX174 has a relatively high mutation rate of 10⁻⁶ substitutions per nucleotide per strand copying. A thirty-fold reduction in the mutation rate was achieved by introducing seven GATC sequences in its genome. This motif allows for methyl-directed mismatch repair and is strongly avoided in nature by ΦX174 and other phages.

Microbiology (medical)Mutation rateGenome ViralDNA Mismatch RepairMicrobiologyGenomeEvolution MolecularBacteriophageGeneticsNucleotideMolecular BiologyEcology Evolution Behavior and SystematicsGeneticschemistry.chemical_classificationBase SequencebiologyDNA virusDNA Methylationbiology.organism_classificationInfectious DiseaseschemistrySingle Stranded DNA VirusDNA ViralMutationDNA mismatch repairBacteriophage phi X 174Infection, Genetics and Evolution
researchProduct

DNA Methylation in Nasal Epithelium: Strengths and Limitations of an Emergent Biomarker for Childhood Asthma

2020

Asthma is one of the most widespread chronic respiratory conditions. This disease primarily develops in childhood and is influenced by different factors, mainly genetics and environmental factors. DNA methylation is an epigenetic mechanism which may represent a bridge between these two factors, providing a tool to comprehend the interaction between genetics and environment. Most epidemiological studies in this field have been conducted using blood samples, although DNA methylation marks in blood may not be reliable for drawing exhaustive conclusions about DNA methylation in the airways. Because of the role of nasal epithelium in asthma and the tissue specificity of DNA methylation, studying…

Mini ReviewDisease030204 cardiovascular system & hematologyBioinformaticsPediatrics03 medical and health sciences0302 clinical medicinechildren030225 pediatricsmedicineAsthmaChildhood asthmaDNA methylationbusiness.industryRespiratory diseaselcsh:RJ1-570lcsh:Pediatricsasthmamedicine.diseaseNasal epitheliumEpigenetic Mechanismnasal epitheliumBiomarkerPediatrics Perinatology and Child HealthDNA methylationbiomarkerbusiness
researchProduct

Histone deacetylase A key enzyme for the binding of regulatory proteins to chromatin

1993

AbstractCore histones can be modified by reversible, posttranslational acetylation of specific lysine residues within the N-terminal protein domains. The dynamic equilibrium of acetylation is maintained by two enzyme activities, histone acetyltransferase and histone deacetylase. Recent data on histone deacetylases and on anionic motifs in chromatin- or DNA-binding regulatory proteins (e.g. transcription factors, nuclear proto-oncogenes) are summarized and united into a hypothesis which attributes a key function to histone deacetylation for the binding of regulatory proteins to chromatin by a transient, specific local increase of the positive charge in the N-terminal domains of nucleosomal c…

Models MolecularBiophysicsBiologyBiochemistryHistone DeacetylasesHistonesHistone H1Structural BiologyHistone H2AHistone methylationGeneticsAnimalsHumansHistone codeHistone octamerHistone deacetylaseMolecular BiologyOncogene proteinHistone deacetylase 2Cell BiologyMolecular biologyChromatinCell biologyHistone acetylationHistone methyltransferaseHistone deacetylaseTranscription factorTranscriptionProtein BindingTranscription FactorsFEBS Letters
researchProduct

Mapping the tRNA binding site on the surface of human DNMT2 methyltransferase.

2012

The DNMT2 enzyme methylates tRNA-Asp at position C38. Because there is no tRNA–Dnmt2 cocrystal structure available, we have mapped the tRNA binding site of DNMT2 by systematically mutating surface-exposed lysine and arginine residues to alanine and studying the tRNA methylation activity and binding of the corresponding variants. After mutating 20 lysine and arginine residues, we identified eight of them that caused large (>4-fold) decreases in catalytic activity. These residues cluster within and next to a surface cleft in the protein, which is large enough to accommodate the tRNA anticodon loop and stem. This cleft is located next to the binding pocket for the cofactor S-adenosyl-l-methion…

Models MolecularMethyltransferaseProtein ConformationLysineMolecular Sequence DataBiologyBiochemistryMethylationCofactorRNA TransferAnimalsHumansAmino Acid SequenceDNA (Cytosine-5-)-MethyltransferasesCloning MolecularAlaninechemistry.chemical_classificationTRNA methylationBinding SitesCircular DichroismTRNA bindingEnzymeDrosophila melanogasterchemistryBiochemistryAmino Acid SubstitutionTransfer RNAbiology.proteinMutagenesis Site-DirectedNucleic Acid ConformationSequence AlignmentBiochemistry
researchProduct

RNA nucleotide methylation

2011

Methylation of RNA occurs at a variety of atoms, nucleotides, sequences and tertiary structures. Strongly related to other posttranscriptional modifications, methylation of different RNA species includes tRNA, rRNA, mRNA, tmRNA, snRNA, snoRNA, miRNA, and viral RNA. Different catalytic strategies are employed for RNA methylation by a variety of RNA-methyltransferases which fall into four superfamilies. This review outlines the different functions of methyl groups in RNA, including biophysical, biochemical and metabolic stabilization of RNA, quality control, resistance to antibiotics, mRNA reading frame maintenance, deciphering of normal and altered genetic code, selenocysteine incorporation,…

Models MolecularRNA methylationRNA-dependent RNA polymeraseRNA ArchaealBiologyMethylationBiochemistryRNA TransferDrug Resistance BacterialRNA Processing Post-TranscriptionalMolecular BiologyGeneticstRNA MethyltransferasesBinding SitesIntronRNANon-coding RNARNA BacterialRNA silencingRNA RibosomalRNA editingProtein BiosynthesisBiocatalysisNucleic Acid ConformationRNARNA ViralSmall nuclear RNAWIREs RNA
researchProduct

Theoretical Study of the Catalytic Mechanism of DNA-(N4-Cytosine)-Methyltransferase from the Bacterium Proteus vulgaris

2010

In this paper the reaction mechanism for methylation of cytosine at the exocyclic N4 position catalyzed by M.PvuII has been explored by means of hybrid quantum mechanics/molecular mechanics (QM/MM) methods. A reaction model was prepared by placing a single cytosine base in the active site of the enzyme. In this model the exocyclic amino group of the base establishes hydrogen bond interactions with the hydroxyl oxygen atom of Ser53 and the carbonyl oxygen atom of Pro54. The reaction mechanism involves a direct methyl transfer from AdoMet to the N4 atom and a proton transfer from this atom to Ser53, which in turn transfers a proton to Asp96. Different timings for the proton transfers and meth…

Models MolecularReaction mechanismProtonbiologyHydrogen bondStereochemistrySite-Specific DNA-Methyltransferase (Cytosine-N4-Specific)Active siteMethylationDNA MethylationPhotochemistryProtein Structure TertiarySurfaces Coatings and FilmsCatalysischemistry.chemical_compoundchemistryBiocatalysisMaterials Chemistrybiology.proteinProteus vulgarisQuantum TheoryPhysical and Theoretical ChemistryCytosineDNAThe Journal of Physical Chemistry B
researchProduct

Structural Characterization of Set1 RNA Recognition Motifs and their Role in Histone H3 Lysine 4 Methylation

2006

Departament de Bioquimica iBiologia Molecular, Universitatde Valencia, C/Dr Moliner 50,46100, Burjassot, SpainThe yeast Set1 histone H3 lysine 4 (H3K4) methyltransferase contains, inaddition to its catalytic SET domain, a conserved RNA recognition motif(RRM1). We present here the crystal structure and the secondary structureassignment in solution of the Set1 RRM1. Although RRM1 has the expectedβαββαβ RRM-fold, it lacks the typical RNA-binding features of thesemodules. RRM1 is not able to bind RNA by itself in vitro, but a constructcombining RRM1 with a newly identified downstream RRM2 specificallybinds RNA. Invivo,H3K4 methylation isnot affectedbyapoint mutation inRRM2 that preserves Set1 s…

Models MolecularRiboswitchHistone H3 Lysine 4Saccharomyces cerevisiae ProteinsRNA-induced transcriptional silencingSurface Properties[SDV]Life Sciences [q-bio]Molecular Sequence DataSaccharomyces cerevisiae[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]BiologyMethylationHistonesStructure-Activity Relationship03 medical and health sciencesStructural BiologyHistone methylation[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Amino Acid SequenceProtein Structure QuaternaryMolecular BiologyConserved Sequence030304 developmental biology0303 health sciencesRNA recognition motifLysine030302 biochemistry & molecular biologyRNARNA FungalHistone-Lysine N-MethyltransferaseNon-coding RNAMolecular biology[SDV] Life Sciences [q-bio]DNA-Binding ProteinsProtein SubunitsBiochemistryHistone methyltransferaseSequence AlignmentProtein BindingTranscription Factors
researchProduct

Psychiatric genome-wide association study analyses implicate neuronal, immune and histone pathways

2015

G.B. and S.N. acknowledge funding support for this work from the National Institute for Health Research (NIHR) Mental Health Biomedical Research Centre at South London and Maudsley NHS Foundation Trust and King's College London. P.H.L. is supported by US National Institute of Mental Health (NIMH) grant K99MH101367. Genome-wide association studies (GWAS) of psychiatric disorders have identified multiple genetic associations with such disorders, but better methods are needed to derive the underlying biological mechanisms that these signals indicate. We sought to identify biological pathways in GWAS data from over 60,000 participants from the Psychiatric Genomics Consortium. We developed an an…

Netherlands Twin Register (NTR)Statistical methodsAutismMedizinLOCIGenome-wide association studyheritabilityGenome-wide association studiesHistonesGenètica mèdica0302 clinical medicineHistone methylationDatabases Genetic2.1 Biological and endogenous factorsPsychologyGWASAetiologyPsychiatric geneticsR2Cbipolar disorderPsychiatry0303 health sciencesDisordersLociDepressionGeneral NeuroscienceMental DisordersMedical geneticsMETHYLATIONBrain3rd-DASSerious Mental IllnessPsychiatric Disorders3. Good healthHistoneMental HealthSchizophreniaMental DisorderCognitive Sciences[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]PromotersBDCBURDENRC0321 Neuroscience. Biological psychiatry. NeuropsychiatryHumanSignal Transductionmedicine.medical_specialtyDISORDERSGenomicsNetwork and Pathway Analysis Subgroup of Psychiatric Genomics ConsortiumBurdenBiologyMethylationArticleBiological pathwayPROMOTERS03 medical and health sciencesDatabasesGeneticmedicineGenetics/dk/atira/pure/keywords/cohort_studies/netherlands_twin_register_ntr_HumansGenetic Predisposition to Diseasehistone methylationBipolar disorderPsiquiatriaAUTISMPsychiatry030304 developmental biologyGenetic associationNeurodevelopmental disorders Donders Center for Medical Neuroscience [Radboudumc 7]Neurology & NeurosurgeryNeuroscience (all)Human GenomeNeurosciencesmedicine.diseaseBrain DisordersGood Health and Well BeingDE-NOVO MUTATIONSPerturbações do Desenvolvimento Infantil e Saúde MentalRC0321SchizophreniaGenome-wide Association StudiesDe-novo mutationsmajor depressionNeuroscience030217 neurology & neurosurgeryGenome-Wide Association Study
researchProduct

Acetylated nucleosome assembly on telomeric DNAs

2003

Abstract The role of histone N-terminal domains on the thermodynamic stability of nucleosomes assembled on several different telomeric DNAs as well as on ‘average’ sequence DNA and on strong nucleosome positioning sequences, has been studied by competitive reconstitution. We find that histone tails hyperacetylation favors nucleosome formation, in a similar extent for all the examined sequences. On the contrary, removal of histone terminal domains by selective trypsinization causes a decrease of nucleosome stability which is smaller for telomeres compared to the other sequences examined, suggesting that telomeric sequences have only minor interactions with histone tails. Micrococcal nuclease…

Nucleosome assemblyBiophysicsBinding CompetitiveBiochemistryHistonesKluyveromycesHistone H1Histone methylationAnimalsHumansMicrococcal NucleaseNucleosomeHistone codeHistone octamerChemistrynucleosomeChlamydomonasOrganic Chemistryhistone acetylationhistone acetylation; nucleosome; nucleosome positioning; telomeres; thermodynamic stabilityAcetylationDNATelomeretelomeresLinker DNANucleosomesProtein Structure TertiaryBiochemistryChromatosomeBiophysicsthermodynamic stabilityThermodynamicsnucleosome positioningBiophysical Chemistry
researchProduct

Hypermethylator phenotype in sporadic colon cancer: study on a population-based series of 582 cases.

2008

Abstract The CpG island methylator phenotype (CIMP) is a distinct phenotype in colorectal cancer, associated with specific clinical, pathologic, and molecular features. However, most of the studies stratified methylation according to two subgroups (CIMP-High versus No-CIMP/CIMP-Low). In our study, we defined three different subgroups of methylation (No-CIMP, CIMP-Low, and CIMP-High) and evaluated the prognostic significance of methylation status on a population-based series of sporadic colon cancers. A total of 582 colon adenocarcinomas were evaluated using methylation-specific PCR for 5 markers (hMLH1, P16, MINT1, MINT2, and MINT31). No-CIMP status was defined as no methylated locus, CIMP-…

OncologyAdultMaleProto-Oncogene Proteins B-rafCancer Researchmedicine.medical_specialtyPathologyColorectal cancerPopulationBiologyAdenocarcinomamedicine.disease_causeProto-Oncogene Proteins p21(ras)Internal medicineProto-Oncogene ProteinsmedicineHumanseducationneoplasmsAgededucation.field_of_studyRelative survivalCpG Island Methylator PhenotypeMicrosatellite instabilityMethylationDNA MethylationMiddle Agedmedicine.diseasePrognosisdigestive system diseasesPhenotypeOncologyDNA methylationColonic NeoplasmsMutationras ProteinsCpG IslandsFemaleMicrosatellite InstabilityKRASCancer research
researchProduct