Search results for " RNA"

showing 10 items of 1405 documents

HEXIM1 Diffusion in the Nucleus Is Regulated by Its Interactions with Both 7SK and P-TEFb

2019

International audience; How nuclear proteins diffuse and find their targets remains a key question in the transcription field. Dynamic proteins in the nucleus are classically subdiffusive and undergo anomalous diffusion, yet the underlying physical mechanisms are still debated. In this study, we explore the contribution of interactions to the generation of anomalous diffusion by the means of fluorescence spectroscopy and simulation. Using interaction-deficient mutants, our study indicates that HEXIM1 interactions with both 7SK RNA and positive transcription elongation factor b are critical for HEXIM1 subdiffusion and thus provides evidence of the effects of protein-RNA interaction on molecu…

Models MolecularAnomalous diffusion[SDV]Life Sciences [q-bio]PopulationBiophysicsPlasma protein bindingDiffusion03 medical and health sciences0302 clinical medicineCell Line Tumor7SK RNAmedicineHumansComputer SimulationPositive Transcriptional Elongation Factor BNuclear proteinP-TEFbeducationComputingMilieux_MISCELLANEOUS030304 developmental biologyCell Nucleus0303 health sciencesMolecular diffusioneducation.field_of_studyChemistryRNA-Binding ProteinsArticles[SDV] Life Sciences [q-bio][SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsSpectrometry Fluorescencemedicine.anatomical_structureBiophysicsRNA Long NoncodingNucleus030217 neurology & neurosurgeryProtein BindingTranscription Factors
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Reiterative transcription initiation from galP2 promoter of Escherichia coli

2000

The expression of gal operon in Escherichia coli is driven by two promoters, P1 and P2 separated by 5 bp. The transcription initiated from the P2 generates a large amount of abortive transcripts to produce a comparable amount of full-length transcript as P1 in vitro. In this study, we investigated the source of the abortive transcripts by employing a quantitative potassium permanganate footprinting method that determines the extent of open promoter complex formation. The extents of open promoter complex formation at the two gal promoters were about the same during the given reaction time while the amount of transcription initiation determined by in vitro transcription assay showed a conside…

Models MolecularCyclic AMP Receptor ProteinTranscription GeneticDNA FootprintingBiophysicsRNA polymerase IIBiochemistryAbortive initiationchemistry.chemical_compoundPotassium PermanganateStructural BiologyRNA polymeraseEscherichia coliGeneticsPromoter Regions GeneticbiologyGeneral transcription factorPromoterDNA-Directed RNA PolymerasesTemplates GeneticMolecular biologyKineticschemistrybiology.proteinRNATranscription factor II FTranscription factor II DCarrier ProteinsTranscription factor II BBiochimica et Biophysica Acta (BBA) - Gene Structure and Expression
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Molecular dissection of human Argonaute proteins by DNA shuffling.

2013

A paramount task in RNA interference research is to decipher the complex biology of cellular effectors, exemplified in humans by four pleiotropic Argonaute proteins (Ago1-Ago4). Here, we exploited DNA family shuffling, a molecular evolution technology, to generate chimeric Ago protein libraries for dissection of intricate phenotypes independently of prior structural knowledge. Through shuffling of human Ago2 and Ago3, we discovered two N-terminal motifs that govern RNA cleavage in concert with the PIWI domain. Structural modeling predicts an impact on protein rigidity and/or RNA-PIWI alignment, suggesting new mechanistic explanations for Ago3's slicing deficiency. Characterization of hybrid…

Models MolecularDNA ComplementaryProtein ConformationRecombinant Fusion ProteinsMolecular Sequence DataDNA RecombinantPiwi-interacting RNASequence alignmentComputational biologyBiologyStructural BiologyMolecular evolutionRNA interferenceConsensus SequenceConsensus sequenceHumansAmino Acid SequenceEukaryotic Initiation FactorsRNA Processing Post-TranscriptionalRNA Small InterferingMolecular BiologyGene LibraryGeneticsSequence Homology Amino AcidRNADNA ShufflingArgonauteDNA shufflingProtein Structure TertiaryMicroRNAsPhenotypeArgonaute ProteinsRNA InterferenceDirected Molecular EvolutionSequence AlignmentNature structuralmolecular biology
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Gain-of-function mutations in IFIH1 cause a spectrum of human disease phenotypes associated with upregulated type I interferon signaling.

2014

The type I interferon system is integral to human antiviral immunity. However, inappropriate stimulation or defective negative regulation of this system can lead to inflammatory disease. We sought to determine the molecular basis of genetically uncharacterized cases of the type I interferonopathy Aicardi-Goutières syndrome, and of other patients with undefined neurological and immunological phenotypes also demonstrating an upregulated type I interferon response. We found that heterozygous mutations in the cytosolic double-stranded RNA receptor gene IFIH1 (MDA5) cause a spectrum of neuro-immunological features consistently associated with an enhanced interferon state. Cellular and biochemica…

Models MolecularInterferon-Induced Helicase IFIH1Molecular Sequence DataHDE NEU PEDElectrophoretic Mobility Shift AssayBiologymedicine.disease_causeNervous System MalformationsReal-Time Polymerase Chain ReactionArticleDEAD-box RNA HelicasesImmune systemAutoimmune Diseases of the Nervous SystemDownregulation and upregulationAnalysis of Variance; Autoimmune Diseases of the Nervous System; Base Sequence; DEAD-box RNA Helicases; Electrophoretic Mobility Shift Assay; Exome; HEK293 Cells; Humans; Interferon Type I; Microsatellite Repeats; Molecular Sequence Data; Mutation; Nervous System Malformations; Real-Time Polymerase Chain Reaction; Sequence Analysis DNA; Signal Transduction; Spectrum Analysis; Models Molecular; Phenotype; GeneticsModelsInterferonGeneticsmedicineHumansExomeMutationAnalysis of VarianceBase SequenceSpectrum AnalysisMolecularRNAMDA5DNASequence Analysis DNAMolecular biology3. Good healthInterferon Tipo IHEK293 CellsPhenotypeInterferon Type IMutationCancer researchSignal transductionSequence AnalysisInterferon type Imedicine.drugMicrosatellite RepeatsSignal TransductionNature genetics
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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
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A modified dinucleotide motif specifies tRNA recognition by TLR7

2014

RNA can function as a pathogen-associated molecular pattern (PAMP) whose recognition by the innate immune system alerts the body to an impending microbial infection. The recognition of tRNA as either self or nonself RNA by TLR7 depends on its modification patterns. In particular, it is known that the presence of a ribose methylated guanosine at position 18, which is overrepresented in self-RNA, antagonizes an immune response. Here, we report that recognition extends to the next downstream nucleotide and the effectively recognized molecular detail is actually a methylated dinucleotide. The most efficient nucleobases combination of this motif includes two purines, while pyrimidines diminish t…

Models MolecularMolecular Sequence DataGuanosineBiologySubstrate Specificitychemistry.chemical_compoundRNA TransferRiboseHumansNucleotideBinding siteLetter to the EditorMolecular BiologyCells Culturedchemistry.chemical_classificationGeneticsBinding SitesInnate immune systemBase Sequencevirus diseasesRNAMethylationToll-Like Receptor 7chemistryTransfer RNANucleic Acid ConformationProtein BindingRNA
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A multifunctional bicupin serves as precursor for a chromosomal protein of Pisum sativum seeds.

2005

The fact that the psp54 gene codes for p16, a seed chromatin protein of Pisum sativum, has been described previously. In the present paper it is shown that p54, the p16 precursor, also exists as a free polypeptide in pea and that it also yields p38, a second polypeptide from the N-terminal region of p54, which is co-localized at a subcellular level with p16. By using antibodies against pea p16 and p38, it was found that these proteins are present in the members of the tribe Viciae examined. Sequence analysis and 3D modelling indicates that p54 proteins belong to the cupin superfamily, and that they are related to sucrose binding proteins and, to a lesser extent, to vicilin-type seed storage…

Models MolecularPhysiologySequence analysisChromosomal Proteins Non-HistoneMolecular Sequence DataPlant ScienceResponse ElementsDNA-binding proteinPisumSativumGene Expression Regulation PlantSequence Analysis ProteinGene expressionStorage proteinAmino Acid SequenceRNA MessengerProtein PrecursorsPromoter Regions GeneticGenePlant Proteinschemistry.chemical_classificationMessenger RNAbiologyPeasfood and beveragesbiology.organism_classificationBiochemistrychemistryMultigene FamilyProtein BiosynthesisSeedsProtein Processing Post-TranslationalSequence AlignmentAbscisic AcidJournal of experimental botany
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Single-Molecule FRET Reveals a Cooperative Effect of Two Methyl Group Modifications in the Folding of Human Mitochondrial tRNALys

2011

Summary Using a combination of advanced RNA synthesis techniques and single molecule spectroscopy, the deconvolution of individual contributions of posttranscriptional modifications to the overall folding and stabilization of human mitochondrial tRNA Lys is described. An unexpected destabilizing effect of two pseudouridines on the native tRNA folding was evidenced. Furthermore, the presence of m 2 G10 alone does not facilitate the folding of tRNA Lys , but a stabilization of the biologically functional cloverleaf shape in conjunction with the principal stabilizing component m 1 A9 exceeds the contribution of m 1 A alone. This constitutes an unprecedented cooperative effect of two nucleotide…

Models MolecularRNA StabilityMolecular Sequence DataClinical BiochemistryContext (language use)BiologyBiochemistryOrganophosphorus CompoundsDrug DiscoveryFluorescence Resonance Energy TransferHumansNucleotideMagnesiumTRNA foldingColoring AgentsMolecular Biologychemistry.chemical_classificationPharmacologyBase SequenceOligonucleotideRNAGeneral MedicineSingle-molecule FRETMitochondriaFolding (chemistry)chemistryBiochemistryTransfer RNABiophysicsNucleic Acid ConformationRNA Transfer LysMolecular MedicinePseudouridineChemistry & Biology
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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
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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
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