Search results for "RNA-Binding Protein"

showing 10 items of 194 documents

m6A modulates neuronal functions and sex determination in Drosophila

2016

N6-methyladenosine RNA (m6A) is a prevalent messenger RNA modification in vertebrates. Although its functions in the regulation of post-transcriptional gene expression are beginning to be unveiled, the precise roles of m6A during development of complex organisms remain unclear. Here we carry out a comprehensive molecular and physiological characterization of the individual components of the methyltransferase complex, as well as of the YTH domain-containing nuclear reader protein in Drosophila melanogaster. We identify the member of the split ends protein family, Spenito, as a novel bona fide subunit of the methyltransferase complex. We further demonstrate important roles of this complex in …

0301 basic medicineGeneticsMessenger RNAMultidisciplinarybiologyProtein familyMethyltransferase complexEffectorRNA-binding proteinbiology.organism_classificationCell biology03 medical and health sciences030104 developmental biology0302 clinical medicineNuclear proteinDrosophila melanogaster030217 neurology & neurosurgeryDrosophila ProteinNature
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From “Cellular” RNA to “Smart” RNA: Multiple Roles of RNA in Genome Stability and Beyond

2018

Coding for proteins has been considered the main function of RNA since the "central dogma" of biology was proposed. The discovery of noncoding transcripts shed light on additional roles of RNA, ranging from the support of polypeptide synthesis, to the assembly of subnuclear structures, to gene expression modulation. Cellular RNA has therefore been recognized as a central player in often unanticipated biological processes, including genomic stability. This ever-expanding list of functions inspired us to think of RNA as a "smart" phone, which has replaced the older obsolete "cellular" phone. In this review, we summarize the last two decades of advances in research on the interface between RNA…

0301 basic medicineGenome instabilityRegulation of gene expressionRNA UntranslatedTranscription GeneticChemistryRNA-Binding ProteinsRNARNA-binding proteinGeneral ChemistryComputational biologyNon-coding RNAArticleGenomic Instability03 medical and health sciences030104 developmental biologyGene Expression RegulationTranscription (biology)RNA interferenceGene expressionHumans570 Life sciences; biologyDNA Breaks Double-StrandedRNA InterferenceDNA Damage
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Molecular partners of hNOT/ALG3, the human counterpart of the Drosophila NOT and yeast ALG3 gene, suggest its involvement in distinct cellular proces…

2018

This study provides first insights into the involvement of hNOT/ALG3, the human counterpart of the Drosophila Neighbour of TID and yeast ALG3 gene, in various putative molecular networks. HNOT/ALG3 encodes two translated transcripts encoding precursor proteins differing in their N-terminus and showing 33% identity with the yeast asparagine-linked glycosylation 3 (ALG3) protein. Experimental evidence for the functional homology of the proteins of fly and man in the N-glycosylation has still to be provided. In this study, using the yeast two-hybrid technique we identify 17 molecular partners of hNOT-1/ALG3-1. We disclose the building of hNOT/ALG3 homodimers and provide experimental evidence f…

0301 basic medicineGlycosylationSaccharomyces cerevisiae ProteinsRNA-binding proteinSaccharomyces cerevisiaeBiologyEndoplasmic ReticulumMannosyltransferases03 medical and health scienceschemistry.chemical_compoundCongenital Disorders of GlycosylationNeoplasmsNuclear Receptor Subfamily 4 Group A Member 2GeneticsAnimalsDrosophila ProteinsHumansMolecular BiologyTranscription factorOSBPGeneGenetics (clinical)Cellular compartmentEndoplasmic reticulumMembrane ProteinsRNA-Binding ProteinsGeneral MedicineLRP1Cell biology030104 developmental biologychemistryNerve DegenerationDrosophilaCarrier ProteinsHuman molecular genetics
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Prenatal exposure to mixtures of xenoestrogens and genome-wide DNA methylation in human placenta

2015

BACKGROUND: In utero exposure to xenostrogens may modify the epigenome. We explored the association of prenatal exposure to mixtures of xenoestrogens and genome-wide placental DNA methylation. MATERIALS & METHODS: Sex-specific associations between methylation changes in placental DNA by doubling the concentration of TEXB-alpha exposure were evaluated by robust multiple linear regression. Two CpG sites were selected for validation and replication in additional male born placentas. RESULTS: No significant associations were found, although the top significant CpGs in boys were located in the LRPAP1, HAGH, PPARGC1B, KCNQ1 and KCNQ1DN genes, previously associated to birth weight, Type 2 diabetes…

0301 basic medicineMaleCancer Researchmedicine.medical_specialtymedicine.medical_treatmentPlacentaADNBiologyEpigenesis GeneticAndrology03 medical and health scienceschemistry.chemical_compoundSex FactorsPregnancyPlacentaInternal medicineGeneticsmedicineBirth WeightHumansPrenatalLDL-Receptor Related Protein-Associated ProteinGeneTEXBEndocrine disruptorsDNA methylationEpigenome xenoestrogensRNA-Binding ProteinsEstrogensMethylationEpigenomeSteroid hormone030104 developmental biologyEndocrinologymedicine.anatomical_structureXenoestrogenCpG sitechemistryPrenatal Exposure Delayed EffectsDNA methylationKCNQ1 Potassium ChannelProgrammingCpG IslandsFemaleThiolester HydrolasesCarrier ProteinsGenome-Wide Association Study
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Genome-wide Trans-ethnic Meta-analysis Identifies Seven Genetic Loci Influencing Erythrocyte Traits and a Role for RBPMS in Erythropoiesis

2017

Genome-wide association studies (GWASs) have identified loci for erythrocyte traits in primarily European ancestry populations. We conducted GWAS meta-analyses of six erythrocyte traits in 71,638 individuals from European, East Asian, and African ancestries using a Bayesian approach to account for heterogeneity in allelic effects and variation in the structure of linkage disequilibrium between ethnicities. We identified seven loci for erythrocyte traits including a locus (RBPMS/GTF2E2) associated with mean corpuscular hemoglobin and mean corpuscular volume. Statistical fine-mapping at this locus pointed to RBPMS at this locus and excluded nearby GTF2E2. Using zebrafish morpholino to evaluat…

0301 basic medicineMaleLinkage disequilibriumAsiaErythrocytesGenome-wide association studyLocus (genetics)RBPMS030105 genetics & heredityBiologyEasternGenomeMedical and Health SciencesArticleLinkage Disequilibrium03 medical and health sciencesGeneticsEthnicityAnimalsHumansErythropoiesisAlleleGenetics (clinical)Loss functionAllelesZebrafishGenetic associationGeneticsGenetics & HeredityAsia EasternHuman GenomeRacial GroupsRNA-Binding ProteinsBioBank Japan ProjectBayes TheoremHematologyBiological SciencesR13. Good healthEurope030104 developmental biologyAfricaFemaleGenome-Wide Association Study
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rbFOX1/MBNL1 competition for CCUG RNA repeats binding contributes to myotonic dystrophy type 1/type 2 differences

2018

Myotonic dystrophy type 1 and type 2 (DM1, DM2) are caused by expansions of CTG and CCTG repeats, respectively. RNAs containing expanded CUG or CCUG repeats interfere with the metabolism of other RNAs through titration of the Muscleblind-like (MBNL) RNA binding proteins. DM2 follows a more favorable clinical course than DM1, suggesting that specific modifiers may modulate DM severity. Here, we report that the rbFOX1 RNA binding protein binds to expanded CCUG RNA repeats, but not to expanded CUG RNA repeats. Interestingly, rbFOX1 competes with MBNL1 for binding to CCUG expanded repeats and overexpression of rbFOX1 partly releases MBNL1 from sequestration within CCUG RNA foci in DM2 muscle ce…

0301 basic medicineModels MolecularProtein Conformation alpha-Helical[SDV]Life Sciences [q-bio]General Physics and AstronomyGene ExpressionRNA-binding proteinCrystallography X-Raychemistry.chemical_compoundMOLECULAR-BASISGene expressionMBNL1Myotonic DystrophyComputingMilieux_MISCELLANEOUSMultidisciplinaryCHLORIDE CHANNELQRNA-Binding ProteinsRecombinant Proteins3. Good healthCell biologyCONGENITAL HEART-DISEASEDrosophila melanogasterThermodynamicsSKELETAL-MUSCLERNA Splicing FactorsCUG REPEATSProtein BindingRNA Splicing Factorsmusculoskeletal diseasesSTEADY-STATEcongenital hereditary and neonatal diseases and abnormalitiesScienceRBFOX1BiologyMyotonic dystrophyBinding CompetitiveGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesmedicineEscherichia coliAnimalsHumansProtein Interaction Domains and MotifsBinding siteNucleotide MotifsMuscle SkeletalSPLICING REGULATOR RBFOX2MUSCLEBLIND PROTEINSBinding SitesPRE-MESSENGER-RNARNAGeneral Chemistrymedicine.diseaseDisease Models AnimalKinetics030104 developmental biologychemistryTRIPLET REPEATRNAProtein Conformation beta-Strand3111 Biomedicine
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In silico discovery of substituted pyrido[2,3-d]pyrimidines and pentamidine-like compounds with biological activity in myotonic dystrophy models

2016

Myotonic dystrophy type 1 (DM1) is a rare multisystemic disorder associated with an expansion of CUG repeats in mutant DMPK (dystrophia myotonica protein kinase) transcripts; the main effect of these expansions is the induction of pre-mRNA splicing defects by sequestering muscleblind-like family proteins (e.g. MBNL1). Disruption of the CUG repeats and the MBNL1 protein complex has been established as the best therapeutic approach for DM1, hence two main strategies have been proposed: targeted degradation of mutant DMPK transcripts and the development of CUG-binding molecules that prevent MBNL1 sequestration. Herein, suitable CUG-binding small molecules were selected using in silico approach…

0301 basic medicineMolecular biologyPhysiologyMutantMyotonic dystrophyDruggabilitylcsh:Medicine01 natural sciencesBiochemistryPhysical ChemistryMyoblastschemistry.chemical_compoundAnabolic AgentsMedicaments--InteraccióAnimal CellsDrug DiscoveryMedicine and Health SciencesMBNL1Drosophila ProteinsMyotonic Dystrophylcsh:ScienceRNA structureConnective Tissue CellsMultidisciplinaryMolecular StructureOrganic CompoundsStem CellsPhysicsRNA-Binding ProteinsBiological activityPhenotypeClimbingMolecular Docking SimulationNucleic acidsChemistryDrosophila melanogasterBiochemistryGenetic DiseasesConnective TissueRNA splicingPhysical SciencesCellular TypesAnatomyLocomotion57 - BiologiaSignal TransductionResearch ArticleBiotechnologyHydrogen bondingcongenital hereditary and neonatal diseases and abnormalitiesIn silicoPrimary Cell CultureComputational biologyBiology010402 general chemistryMyotonic dystrophyMyotonin-Protein KinaseDrug interactionsSmall Molecule Libraries03 medical and health sciencesStructure-Activity RelationshipmedicineAnimalsHumansRNA MessengerEnllaços d'hidrogenClinical GeneticsChemical PhysicsBiology and life sciencesChemical BondingBiological Locomotionlcsh:ROrganic ChemistryEstructura molecularChemical CompoundsHydrogen BondingCell BiologyFibroblastsmedicine.disease0104 chemical sciencesBenzamidinesAlternative SplicingDisease Models AnimalMacromolecular structure analysis030104 developmental biologyPyrimidinesBiological TissuechemistrySmall MoleculesRNAlcsh:QTrinucleotide Repeat ExpansionMolecular structure
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Defining Ewing and Ewing-like small round cell tumors (SRCT): The need for molecular techniques in their categorization and differential diagnosis. A…

2016

Abstract Background Differentiation of Ewing sarcoma family of tumors (ESFT) and Ewing-like tumors remains problematic. Certain ESFT with morphological and immunohistochemical (IHC) profiles lack the EWSR1-ETS transcript. To improve diagnostic accuracy we investigated the presence of several specific transcripts in 200 small round cell tumors (SRCT) displaying ESFT morphology and immunophenotype in which EWSR1 FISH analysis was non-informative or negative. Design 200 tumors (formalin-fixed, paraffin-embedded) were analyzed by RT-PCR. All tumors were tested for EWSR1-ETS , EWSR1 / WT1 , PAX3 / 7-FOX01 or SYT / SSX transcripts, and the negative tumors were subsequently analyzed for CIC / DUX4…

0301 basic medicinePathologymedicine.medical_specialtyOncogene Proteins FusionDesmoplastic small-round-cell tumorCD99Sarcoma EwingBiologyTranslocation GeneticPathology and Forensic MedicineDiagnosis DifferentialFusion gene03 medical and health sciences0302 clinical medicineImmunophenotypingBiomarkers TumormedicineHumansPathology MolecularIn Situ Hybridization FluorescenceRNA-Binding ProteinsGeneral Medicinemedicine.diseaseSynovial sarcoma030104 developmental biology030220 oncology & carcinogenesisSarcoma Small CellImmunohistochemistryCalmodulin-Binding ProteinsSarcomaRNA-Binding Protein EWSDifferential diagnosisAnnals of Diagnostic Pathology
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eIF5A facilitates translation termination globally and promotes the elongation of many non polyproline-specific tripeptide sequences

2017

Abstract eIF5A is an essential protein involved in protein synthesis, cell proliferation and animal development. High eIF5A expression is observed in many tumor types and has been linked to cancer metastasis. Recent studies have shown that eIF5A facilitates the translation elongation of stretches of consecutive prolines. Activated eIF5A binds to the empty E-site of stalled ribosomes, where it is thought to interact with the peptidyl-tRNA situated at the P-site. Here, we report a genome-wide analysis of ribosome stalling in Saccharomyces cerevisiae eIF5A depleted cells using 5Pseq. We confirm that, in the absence of eIF5A, ribosomes stall at proline stretches, and extend previous studies by …

0301 basic medicinePeptidyl transferaseProlineCytoskeleton organizationAmino Acid MotifsSaccharomyces cerevisiaePeptide Chain Elongation TranslationalSaccharomyces cerevisiaeBioinformaticsRibosomeGTP Phosphohydrolases03 medical and health sciences0302 clinical medicinePeptide Initiation FactorsGene Expression Regulation FungalGeneticsProtein biosynthesisHumansMolecular BiologyPolyproline helixBinding SitesbiologyRNA-Binding Proteinsbiology.organism_classificationStop codonCell biology030104 developmental biologybiology.proteinGenome FungalHydrophobic and Hydrophilic InteractionsRibosomesEIF5A030217 neurology & neurosurgeryProtein BindingNucleic Acids Research
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Beyond the Transport Function of Import Receptors: What’s All the FUS about?

2018

Nuclear import receptors are central players in transporting protein cargoes into the nucleus. Moving beyond this role, four newly published articles describe a function in regulating supramolecular assemblies by fine-tuning the phase separating properties of RNA-binding proteins, which has implications for a variety of devastating neurodegenerative disorders.

0301 basic medicineProteomeActive Transport Cell NucleusReceptors Cytoplasmic and NuclearBiologyKaryopherinsModels BiologicalGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesmedicineAnimalsHumansReceptorRNA metabolismCell NucleusAmyotrophic Lateral SclerosisRNA-Binding ProteinsNeurodegenerative Diseases3. Good healthCell biologyDNA-Binding ProteinsCell nucleus030104 developmental biologymedicine.anatomical_structureRNARNA-Binding Protein FUSNuclear transportNucleusFunction (biology)Cell
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