Search results for "Transfer"

showing 10 items of 5271 documents

Direct Visualization of the Conformational Dynamics of Single Influenza Hemagglutinin Trimers

2018

Influenza hemagglutinin (HA) is the canonical type I viral envelope glycoprotein and provides a template for the membrane-fusion mechanisms of numerous viruses. The current model of HA-mediated membrane fusion describes a static "spring-loaded" fusion domain (HA2) at neutral pH. Acidic pH triggers a singular irreversible conformational rearrangement in HA2 that fuses viral and cellular membranes. Here, using single-molecule Förster resonance energy transfer (smFRET)-imaging, we directly visualized pH-triggered conformational changes of HA trimers on the viral surface. Our analyses reveal reversible exchange between the pre-fusion and two intermediate conformations of HA2. Acidification of p…

0301 basic medicineProtein ConformationHemagglutinin (influenza)Hemagglutinin Glycoproteins Influenza VirusBiologyArticleGeneral Biochemistry Genetics and Molecular BiologyReaction coordinate03 medical and health sciencesViral envelopeInfluenza HumanFluorescence Resonance Energy TransferHumansDynamic equilibriumFusionCell MembraneLipid bilayer fusionHydrogen-Ion ConcentrationVirus InternalizationSingle Molecule ImagingHEK293 CellsHemagglutinins030104 developmental biologyMembraneFörster resonance energy transferA549 CellsInfluenza A virusBiophysicsbiology.proteinProtein BindingCell
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The RNA methyltransferase Dnmt2 methylates DNA in the structural context of a tRNA

2016

The amino acid sequence of Dnmt2 is very similar to the catalytic domains of bacterial and eukaryotic DNA-(cytosine 5)-methyltransferases, but it efficiently catalyzes tRNA methylation, while its DNA methyltransferase activity is the subject of controversial reports with rates varying between zero and very weak. By using composite nucleic acid molecules as substrates, we surprisingly found that DNA fragments, when presented as covalent DNA-RNA hybrids in the structural context of a tRNA, can be more efficiently methylated than the corresponding natural tRNA substrate. Furthermore, by stepwise development of tRNAAsp, we showed that this natural Dnmt2 substrate could be engineered to employ R…

0301 basic medicineRNA methylationBiologyMethylationCytosineMiceStructure-Activity Relationship03 medical and health scienceschemistry.chemical_compoundRNA Transferenzyme kineticsAnimalsHumansDNA (Cytosine-5-)-MethyltransferasesGuide RNA5-methylcytosinetRNAMolecular Biologymodification pathway crosstalkTRNA methylationRNADNACell BiologyMethylationDNA MethylationRNA modification5-Methylcytosine030104 developmental biologyBiochemistrychemistryTransfer RNARNA methylationNucleic Acid ConformationDnmt2DNAResearch Paper
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MODOMICS: a database of RNA modification pathways. 2017 update

2017

Abstract MODOMICS is a database of RNA modifications that provides comprehensive information concerning the chemical structures of modified ribonucleosides, their biosynthetic pathways, the location of modified residues in RNA sequences, and RNA-modifying enzymes. In the current database version, we included the following new features and data: extended mass spectrometry and liquid chromatography data for modified nucleosides; links between human tRNA sequences and MINTbase - a framework for the interactive exploration of mitochondrial and nuclear tRNA fragments; new, machine-friendly system of unified abbreviations for modified nucleoside names; sets of modified tRNA sequences for two bact…

0301 basic medicineRNA methylationBiologycomputer.software_genreMass Spectrometry03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA TransferEpitranscriptomicsTerminology as TopicRNA modificationDatabases GeneticGeneticsDatabase IssueHumanschemistry.chemical_classificationDatabase2'-O-methylationRNA030104 developmental biologyEnzymechemistry030220 oncology & carcinogenesisTransfer RNARNARibonucleosidesN6-MethyladenosinecomputerChromatography LiquidNucleic Acids Research
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Statistically robust methylation calling for whole-transcriptome bisulfite sequencing reveals distinct methylation patterns for mouse RNAs

2017

AbstractCytosine-5 RNA methylation plays an important role in several biologically and pathologically relevant processes. However, owing to methodological limitations, the transcriptome-wide distribution of this mark has remained largely unknown. We previously established RNA bisulfite sequencing as a method for the analysis of RNA cytosine-5 methylation patterns at single-base resolution. More recently, next-generation sequencing has provided opportunities to establish transcriptome-wide maps of this modification. Here we present a computational approach that integrates tailored filtering and data-driven statistical modeling to eliminate many of the artifacts that are known to be associate…

0301 basic medicineRNA methylationBisulfite sequencingMethodComputational biologyBiologyTranscriptome03 medical and health sciencesMiceRNA modificationsRNA TransferRNA Ribosomal 28SGeneticsm5CAnimalsHumansRNA MessengerRNA Processing Post-TranscriptionalRNA-Directed DNA MethylationBisulfite sequencingGenetics (clinical)GeneticsHigh-Throughput Nucleotide SequencingRNAMethyltransferasesMethylationRibosomal RNADNA Methylation030104 developmental biologyTransfer RNADNA methylationIllumina Methylation AssayTranscriptome
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Mechanism and biological role of Dnmt2 in Nucleic Acid Methylation

2016

ABSTRACT A group of homologous nucleic acid modification enzymes called Dnmt2, Trdmt1, Pmt1, DnmA, and Ehmet in different model organisms catalyze the transfer of a methyl group from the cofactor S-adenosyl-methionine (SAM) to the carbon-5 of cytosine residues. Originally considered as DNA MTases, these enzymes were shown to be tRNA methyltransferases about a decade ago. Between the presumed involvement in DNA modification-related epigenetics, and the recent foray into the RNA modification field, significant progress has characterized Dnmt2-related research. Here, we review this progress in its diverse facets including molecular evolution, structural biology, biochemistry, chemical biology,…

0301 basic medicineRetroelementsRNA methylationChemical biologyReviewBiologyMethylationCatalysisEpigenesis GeneticSubstrate Specificity03 medical and health scienceschemistry.chemical_compoundStructure-Activity RelationshipNucleic AcidsAnimalsHumansEpigeneticsDNA (Cytosine-5-)-MethyltransferasesGene SilencingMolecular BiologytRNAPhylogenyGeneticsNucleic acid methylationDNA methylationBinding SitesepigeneticsCell BiologyTRNA Methyltransferasesmethylcytidine030104 developmental biologyCell Transformation NeoplasticBiochemistrychemistryStructural biologyGene Expression RegulationNucleic acidRNA methylationDNAProtein BindingRNA Biology
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Peripherin-2 differentially interacts with cone opsins in outer segments of cone photoreceptors

2016

Peripherin-2 is a glycomembrane protein exclusively expressed in the light-sensing compartments of rod and cone photoreceptors designated as outer segments (OS). Mutations in peripherin-2 are associated with degenerative retinal diseases either affecting rod or cone photoreceptors. While peripherin-2 has been extensively studied in rods, there is only little information on its supramolecular organization and function in cones. Recently, we have demonstrated that peripherin-2 interacts with the light detector rhodopsin in OS of rods. It remains unclear, however, if peripherin-2 also binds to cone opsins. Here, using a combination of co-immunoprecipitation analyses, transmission electron micr…

0301 basic medicineRhodopsinOpsingenetic structuresmacromolecular substances030105 genetics & heredityBiologymedicine.disease_causeRetinaMice03 medical and health scienceschemistry.chemical_compoundImmunolabelingMicroscopy Electron TransmissionAntigens NeoplasmFluorescence Resonance Energy TransferGeneticsmedicineAnimalsHumansPeripherin 2Molecular BiologyGenetics (clinical)MutationRetinal DegenerationRetinalGeneral MedicineCone Opsinseye diseases030104 developmental biologyFörster resonance energy transfernervous systemchemistryRhodopsinMutationRetinal Cone Photoreceptor CellsBiophysicsbiology.proteinsense organsProtein BindingVisual phototransductionHuman Molecular Genetics
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DICER- and MMSET-catalyzed H4K20me2 recruits the nucleotide excision repair factor XPA to DNA damage sites

2017

The endoribonuclease DICER facilitates chromatin decondensation during lesion recognition following UV exposure. Chitale and Richly show that DICER mediates the recruitment of the methyltransferase MMSET, which catalyzes the dimethylation of histone H4 at lysine 20 and facilitates the recruitment of the nucleotide excision repair factor XPA.

0301 basic medicineRibonuclease IIIDNA RepairDNA damageDNA repairUltraviolet Raysgenetic processes27Article24DEAD-box RNA HelicasesHistones03 medical and health sciencesCell Line TumorHumansResearch ArticlesbiologyLysinefungiEndoribonuclease Dicerfood and beverages37Cell BiologyDNA Repair PathwayHistone-Lysine N-MethyltransferaseCell biologyChromatinXeroderma Pigmentosum Group A ProteinRepressor Proteinsenzymes and coenzymes (carbohydrates)030104 developmental biologyHistoneHEK293 Cellsbiology.proteinBiocatalysisDicerNucleotide excision repairDNA DamageThe Journal of Cell Biology
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Quantitative characterization of translational riboregulators using an in vitro transcription–translation system

2018

Riboregulators are short RNA sequences that, upon binding to a ligand, change their secondary structure and influence the expression rate of a downstream gene. They constitute an attractive alternative to transcription factors for building synthetic gene regulatory networks because they can be engineered de novo. However, riboregulators are generally designed in silico and tested in vivo, which provides little quantitative information about their performances, thus hindering the improvement of design algorithms. Here we show that a cell-free transcription-translation (TX-TL) system provides valuable information about the performances of in silico designed riboregulators. We first propose a …

0301 basic medicineRiboregulator[SDV.BIO]Life Sciences [q-bio]/BiotechnologyTranscription GeneticIn silicoBiomedical EngineeringComputational biologyReal-Time Polymerase Chain ReactionRibosomeBiochemistry Genetics and Molecular Biology (miscellaneous)FluorescenceSynthetic biologyViral Proteins03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA Transfer[CHIM]Chemical SciencesQH426GeneTranscription factor030304 developmental biology0303 health sciencesCell-free protein synthesisCell-Free SystemModels GeneticChemistryActivator (genetics)030302 biochemistry & molecular biologyRNADNADNA-Directed RNA PolymerasesGeneral MedicineCell-free protein synthesisMolecular machine3. Good health030104 developmental biologyGene Expression RegulationGenetic TechniquesProtein BiosynthesisRNA translational riboregulatorNucleic Acid ConformationRNAIn vitro synthetic biology5' Untranslated Regions030217 neurology & neurosurgeryDNA
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The interactions between host glycobiology, bacterial microbiota, and viruses in the gut

2018

Rotavirus (RV) and norovirus (NoV) are the major etiological agents of viral acute gastroenteritis worldwide. Host genetic factors, the histo-blood group antigens (HBGA), are associated with RV and NoV susceptibility and recent findings additionally point to HBGA as a factor modulating the intestinal microbial composition. In vitro and in vivo experiments in animal models established that the microbiota enhances RV and NoV infection, uncovering a triangular interplay between RV and NoV, host glycobiology, and the intestinal microbiota that ultimately influences viral infectivity. Studies on the microbiota composition in individuals displaying different RV and NoV susceptibilities allowed th…

0301 basic medicineRotavirus030106 microbiologylcsh:QR1-502MicrobiologiaReviewBiologymedicine.disease_causelcsh:MicrobiologyMicrobiology03 medical and health sciencesSecretorAntigenstomatognathic systemVirologyRotavirusHisto-blood group antigens (HBGAs)medicineAnimalsHumansGlycomicsInfectivityGlycobiologyHost (biology)MicrobiotaNorovirusAcute gastroenteritisGastroenteritisVirusGastrointestinal Tract030104 developmental biologyInfectious DiseasesHost susceptibilityHost-Pathogen InteractionsFucosyltransferase-2 gene (FUT2)NorovirusReceptors VirusMicrobiota composition
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Role of glutathione in the regulation of epigenetic mechanisms in disease

2017

Epigenetics is a rapidly growing field that studies gene expression modifications not involving changes in the DNA sequence. Histone H3, one of the basic proteins in the nucleosomes that make up chromatin, is S-glutathionylated in mammalian cells and tissues, making Gamma-L-glutamyl-L-cysteinylglycine, glutathione (GSH), a physiological antioxidant and second messenger in cells, a new post-translational modifier of the histone code that alters the structure of the nucleosome. However, the role of GSH in the epigenetic mechanisms likely goes beyond a mere structural function. Evidence supports the hypothesis that there is a link between GSH metabolism and the control of epigenetic mechanisms…

0301 basic medicineS-AdenosylmethionineEpigenetic regulation of neurogenesisADNBiologyBiochemistryEpigenesis GeneticHistones03 medical and health sciencesHistone H3Epigenetics of physical exerciseHistonasNeoplasmsPhysiology (medical)AnimalsHumansHistone codeEpigeneticsCancer epigeneticsEpigenomicsMetabolic SyndromeGenNeurodegenerative DiseasesDNA MethylationGlutathioneGenéticaNucleosomesMicroRNAs030104 developmental biologyBiochemistryHistone methyltransferaseProteínaEpigenéticaProtein Processing Post-TranslationalFree Radical Biology and Medicine
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