Search results for "RNA-binding protein"

showing 10 items of 194 documents

Small RNA‐binding protein RapZ mediates cell envelope precursor sensing and signaling in Escherichia coli

2019

Abstract The RNA‐binding protein RapZ cooperates with small RNAs (sRNAs) GlmY and GlmZ to regulate the glmS mRNA in Escherichia coli. Enzyme GlmS synthesizes glucosamine‐6‐phosphate (GlcN6P), initiating cell envelope biosynthesis. GlmZ activates glmS expression by base‐pairing. When GlcN6P is ample, GlmZ is bound by RapZ and degraded through ribonuclease recruitment. Upon GlcN6P depletion, the decoy sRNA GlmY accumulates through a previously unknown mechanism and sequesters RapZ, suppressing GlmZ decay. This circuit ensures GlcN6P homeostasis and thereby envelope integrity. In this work, we identify RapZ as GlcN6P receptor. GlcN6P‐free RapZ stimulates phosphorylation of the two‐component sy…

Small RNAsmall regulatory RNAcell envelope precursor glucosamine‐6‐phosphatemedicine.disease_causenegative feedback loopmetabolite sensing0302 clinical medicinetwo-component system QseE-QseFRNA-binding protein RapZRNA‐binding protein RapZGlucosamine0303 health sciencesbiologyEscherichia coli ProteinsGeneral NeuroscienceRNA-Binding ProteinsArticlesRNA BiologyMicrobiology Virology & Host Pathogen InteractionReceptors AdrenergicCell biologyDNA-Binding ProteinsRNA BacterialTransfer RNAPhosphorylationCell envelopeSignal TransductionGlucose-6-PhosphateGeneral Biochemistry Genetics and Molecular BiologyArticletwo‐component system QseE‐QseF03 medical and health sciencesBacterial Proteinscell envelope precursorEscherichia colimedicineRNA MessengerRibonucleaseMolecular BiologyEscherichia coli030304 developmental biologyMessenger RNAGeneral Immunology and MicrobiologyBinding proteinsmall RNAs GlmY and GlmZGene Expression Regulation BacterialMicroreviewRNA binding proteincell envelope precursor glucosamine-6-phosphatetwo-component systembiology.proteinRNA Small Untranslated030217 neurology & neurosurgeryThe EMBO Journal
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Post-Transcriptional Regulation of Human Inducible Nitric-Oxide Synthase Expression by the Jun N-terminal Kinase

2007

Human inducible nitric-oxide synthase (iNOS) expression is regulated both at transcriptional and post-transcriptional levels. In the present study, the effect of Jun N-terminal kinase (JNK) on human iNOS expression was investigated. In A549/8 human alveolar epithelial cells, both the inhibition of JNK by a pharmacological inhibitor anthra[1,9-cd]pyrazol-6(2H)-one1,9-pyrazoloanthrone (SP600125) and small interfering RNA (siRNA)-mediated down-regulation of JNK led to a reduction of iNOS mRNA and protein expression. iNOS promoter activity was not affected by these treatments. Hence, JNK seems to regulate iNOS expression through post-transcriptional mechanisms by stabilizing iNOS mRNA. Our labo…

Small interfering RNARNA Stabilityp38 mitogen-activated protein kinasesDown-RegulationNitric Oxide Synthase Type IIRNA-binding proteinNitric Oxidep38 Mitogen-Activated Protein KinasesGene Expression Regulation EnzymologicCell LineTristetraprolinHumansPhosphorylationRNA Small InterferingPromoter Regions GeneticPost-transcriptional regulationAnthracenesPharmacologyRegulation of gene expressionMessenger RNAbiologyChemistryKinaseJNK Mitogen-Activated Protein KinasesEpithelial Cellsrespiratory systemMolecular biologyPulmonary AlveoliNitric oxide synthasebiology.proteinCytokinesMolecular MedicineSignal TransductionMolecular Pharmacology
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2021

Arginine-glycine(-glycine) (RG/RGG) regions are highly abundant in RNA-binding proteins and involved in numerous physiological processes. Aberrant liquid-liquid phase separation (LLPS) and stress granule (SGs) association of RG/RGG regions in the cytoplasm have been implicated in several neurodegenerative disorders. LLPS and SG association of these proteins is regulated by the interaction with nuclear import receptors, such as transportin-1 (TNPO1), and by post-translational arginine methylation. Strikingly, many RG/RGG proteins harbour potential phosphorylation sites within or close to their arginine methylated regions, indicating a regulatory role. Here, we studied the role of phosphoryla…

Stress granuleArginineChemistryTransportin 1PhosphorylationRNA-binding proteinMethylationProtein kinase ABiochemistry Genetics and Molecular Biology (miscellaneous)Molecular BiologyBiochemistryCIRBPCell biologyFrontiers in Molecular Biosciences
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A homolog of the putative tumor suppressor QM in the sponge Suberites domuncula: downregulation during the transition from immortal to mortal (apopto…

1999

Abstract The activation of components of the transcription factors such as AP-1 or c-jun is essential for a physiological response of metazoan cells during aging. The activity of such proto-oncoproteins is under enzymatic control. The function of c-jun is additionally modulated by the QM protein. Here, we studied the expression of the gene, encoding the QM-like protein in the sponge Suberites domuncula . These animals contain high levels of telomerase in their somatic cells. To understand the switch from telomerase-positive immortal cells to telomerase-negative mortal cells which undergo apoptosis, the expression of the QM-like gene was measured in this system. The cDNA, termed QMSD , encod…

TelomeraseMolecular Sequence DataDown-RegulationGene ExpressionApoptosisDownregulation and upregulationComplementary DNAAnimalsHumansAmino Acid SequenceRNA MessengerCloning MolecularTranscription factorGenePhylogenyBase Sequencebiologyc-junProteinsRNA-Binding ProteinsCell BiologyGeneral Medicinebiology.organism_classificationMolecular biologyPoriferaSuberites domunculaOpen reading frameProtein BiosynthesisCarrier ProteinsDevelopmental BiologyTissue and Cell
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Dendritic cell aggresome-like-induced structure formation and delayed antigen presentation coincide in influenza virus-infected dendritic cells.

2005

Abstract Influenza virus infection induces maturation of murine dendritic cells (DCs), which is most important for the initiation of an immune response. However, in contrast to EL-4 and MC57 cells, DCs present viral CTL epitopes with a delay of up to 10 h. This delay in Ag presentation coincides with the up-regulation of MHC class I molecules as well as costimulatory molecules on the cell surface and the accumulation of newly synthesized ubiquitinated proteins in large cytosolic structures, called DC aggresome-like-induced structures (DALIS). These structures were observed previously after LPS-induced maturation of DCs, and it was speculated that they play a role in the regulation of MHC cl…

Time FactorsImmunologyAntigen presentationCellAntigen-Presenting CellsEpitopes T-Lymphocytechemical and pharmacologic phenomenaBone Marrow CellsVirusCell LineMiceImmune systemCell Line TumorMHC class ImedicineImmunology and AllergyAnimalsHumansReceptors ImmunologicCells CulturedAntigen PresentationMice Inbred C3HbiologyUbiquitinViral Core ProteinsRNA-Binding ProteinsCell DifferentiationDendritic cellDendritic CellsNucleocapsid ProteinsVirologyToll-Like Receptor 2Cell biologyNucleoproteinMice Inbred C57BLToll-Like Receptor 4Aggresomemedicine.anatomical_structureNucleoproteinsInfluenza A virusbiology.proteinCytoplasmic StructuresT-Lymphocytes CytotoxicJournal of immunology (Baltimore, Md. : 1950)
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TREND-DB—a transcriptome-wide atlas of the dynamic landscape of alternative polyadenylation

2020

AbstractAlternative polyadenylation (APA) profoundly expands the transcriptome complexity. Perturbations of APA can disrupt biological processes, ultimately resulting in devastating disorders. A major challenge in identifying mechanisms and consequences of APA (and its perturbations) lies in the complexity of RNA 3’end processing, involving poorly conserved RNA motifs and multi-component complexes consisting of far more than 50 proteins. This is further complicated in that RNA 3’end maturation is closely linked to transcription, RNA processing, and even epigenetic (histone/DNA/RNA) modifications. Here we present TREND-DB (http://shiny.imbei.uni-mainz.de:3838/trend-db), a resource cataloging…

Transcription GeneticPolyadenylationAcademicSubjects/SCI00010educationMiRNA bindingRNA-binding proteinComputational biologyBiologyPolyadenylationTranscriptomeUser-Computer Interface03 medical and health sciences0302 clinical medicineRNA interferenceTranscription (biology)Databases GeneticGeneticsHumansDatabase Issue3' Untranslated RegionsGene030304 developmental biologyRegulation of gene expressionInternet0303 health sciencesCleavage And Polyadenylation Specificity FactorRNAGene Expression RegulationTranscriptome030217 neurology & neurosurgeryNucleic Acids Research
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The Kelch protein NS1-BP interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control

2007

Alpha-enolase is a key glycolytic enzyme that plays a functional role in several physiological processes depending on the cellular localization. The enzyme is mainly localized in the cytoplasm whereas an alternative translated form, named MBP-1, is predominantly nuclear. The MBP-1 protein has been characterized as a c-Myc promoter binding protein that negatively controls transcription. In the present study, we identified the kelch protein NS1-BP as one of the alpha-enolase/MBP-1 partners by using a yeast two-hybrid screening. Although NS1-BP has been originally described as a protein mainly localized in the nucleus, we provide evidence that NS1-BP also interacts with actin in human cells, a…

Transcription GeneticTranscription FactorGlycolysiAlpha-enolaseKelch proteinsRNA-Binding ProteinHeLa CellChlorocebus aethiopsTranscriptional regulationPromoter Regions GeneticCellular localizationNuclear ProteinbiologyNuclear ProteinsRNA-Binding ProteinsCell biologyDNA-Binding ProteinsProtein TransportCOS CellsYeast two-hybrid assayGlycolysisHumanProtein BindingSubcellular FractionsImmunoprecipitationDNA-Binding ProteinTwo-hybrid screeningEnolaseChlorocebus aethiopProto-Oncogene Proteins c-mycCOS CellBiomarkers TumorAnimalsHumansKelch proteinMolecular BiologyActinTumor Suppressor ProteinAnimalTumor Suppressor ProteinsBinding proteinc-Myc transcriptionCell BiologyMolecular biologyActinsKelch proteinSubcellular FractionSettore BIO/18 - GeneticaGene Expression RegulationCytoplasmPhosphopyruvate Hydratasebiology.proteinHeLa CellsTranscription FactorsBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery

2004

12 páginas, 7 figuras, 1 tabla. Material suplementario en: https://doi.org/10.1016/S0092-8674(03)01025-0. The SUS1 sequences have been deposited in GenBank with the accession number AY278445.

Transcriptional ActivationNucleocytoplasmic Transport ProteinsDNA ComplementarySaccharomyces cerevisiae ProteinsMolecular Sequence DataActive Transport Cell NucleusPorinsRNA polymerase IIBiologyGeneral Biochemistry Genetics and Molecular BiologyFungal ProteinsTranscription (biology)AcetyltransferasesGene Expression Regulation FungalYeastsGene expressionGenes RegulatorTranscriptional regulationAmino Acid SequenceRNA MessengerNuclear proteinPromoter Regions GeneticHistone AcetyltransferasesRegulation of gene expressionCell NucleusBase SequenceBiochemistry Genetics and Molecular Biology(all)Nuclear ProteinsRNA-Binding ProteinsMolecular biologyCell biologySAGA complexRibonucleoproteinsbiology.proteinNuclear PoreGenes LethalChromatin immunoprecipitation
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Fertility and Polarized Cell Growth Depends on eIF5A for Translation of Polyproline-Rich Formins in Saccharomyces cerevisiae

2014

eIF5A is an essential and evolutionary conserved translation elongation factor, which has recently been proposed to be required for the translation of proteins with consecutive prolines. The binding of eIF5A to ribosomes occurs upon its activation by hypusination, a modification that requires spermidine, an essential factor for mammalian fertility that also promotes yeast mating. We show that in response to pheromone, hypusinated eIF5A is required for shmoo formation, localization of polarisome components, induction of cell fusion proteins, and actin assembly in yeast. We also show that eIF5A is required for the translation of Bni1, a proline-rich formin involved in polarized growth during …

TranslationSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaePeptide Chain Elongation TranslationalForminsRNA-binding proteinSaccharomyces cerevisiaeInvestigationsPeptide Initiation FactorsMorphogenesisGeneticsQc-SNARE ProteinsPolyproline helixPolarisomeGeneticsMatingbiologyMicrofilament ProteinsMembrane ProteinsRNA-Binding ProteinsTranslation (biology)Polarized growthbiology.organism_classificationActinsProtein Structure TertiaryCell biologyCytoskeletal ProteinsMating of yeastForminsMutationbiology.proteinEIF5APeptidesRibosomesEIF5A
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dsRNA induces apoptosis through an atypical death complex associating TLR3 to caspase-8

2012

Toll-like receptor 3 (TLR3) is a pattern-recognition receptor known to initiate an innate immune response when stimulated by double-stranded RNA (dsRNA). Components of TLR3 signaling, including TIR domain-containing adapter inducing IFN-α (TRIF), have been demonstrated to contribute to dsRNA-induced cell death through caspase-8 and receptor interacting protein (RIP)1 in various human cancer cells. We provide here a detailed analysis of the caspase-8 activating machinery triggered in response to Poly(I:C) dsRNA. Engagement of TLR3 by dsRNA in both type I and type II lung cancer cells induces the formation of an atypical caspase-8-containing complex that is devoid of classical death receptors…

Ubiquitin-Protein LigasesvirusesApoptosischemical and pharmacologic phenomenaInhibitor of Apoptosis ProteinsCell Line TumorHumansFADDMolecular BiologyRNA Double-StrandedDeath domainCaspase 8Original PaperbiologyUbiquitinationRNA-Binding Proteinshemic and immune systemsMDA5Cell BiologyTNF Receptor-Associated Factor 2Fas receptorTRADDBaculoviral IAP Repeat-Containing 3 ProteinTNF Receptor-Associated Death Domain ProteinToll-Like Receptor 3Cell biologyNuclear Pore Complex ProteinsUbiquitin ligase complexDeath-inducing signaling complexTLR3biology.proteinSignal TransductionCell Death & Differentiation
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