Search results for "RNA binding"

showing 10 items of 21 documents

Analysis of interaction between messenger RNA encoding H3.3 histone variant and pippin protein by biolayer interferometry

2013

RNA Binding ProteinBLISettore BIO/10 - BiochimicaHistone VariantSettore BIO/06 - Anatomia Comparata E Citologia
researchProduct

RNA-Binding Proteins which interact with mRNAs for H1° and H3.3 histone variants

2014

RNA Binding ProteinSettore BIO/10 - BiochimicaSettore BIO/06 - Anatomia Comparata E CitologiaHistone Variants
researchProduct

REGULATION OF THE EXPRESSION OF RNA-BINDING PROTEINS IN DEVELOPING AND ADULT RAT BRAINS: ROLE OF THYROID HORMONES

2005

RNA binding proteins adult rat brains thyroid hormones
researchProduct

Identificazione di proteine che interagiscono con il messaggero dell’istone H1° nel cervello di ratto in sviluppo

2013

Settore BIO/10 - BiochimicaRNA Binding ProteinsSettore BIO/06 - Anatomia Comparata E Citologia
researchProduct

Histone H1° RNA-binding proteins in developing rat brain.

2011

Settore BIO/10 - BiochimicaRNA Binding proteins histone variants
researchProduct

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
researchProduct

Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator

2019

Abstract Posttranscriptional RNA modifications occur in all domains of life. Modifications of anticodon bases are of particular importance for ribosomal decoding and proteome homeostasis. The Elongator complex modifies uridines in the wobble position and is highly conserved in eukaryotes. Despite recent insights into Elongator's architecture, the structure and function of its regulatory factor Kti12 have remained elusive. Here, we present the crystal structure of Kti12′s nucleotide hydrolase domain trapped in a transition state of ATP hydrolysis. The structure reveals striking similarities to an O-phosphoseryl-tRNA kinase involved in the selenocysteine pathway. Both proteins employ similar …

TRNA modificationSaccharomyces cerevisiae ProteinsProtein ConformationWobble base pairSaccharomyces cerevisiaeBiologyChaetomiumCrystallography X-Ray03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA TransferATP hydrolysisGeneticsRNA and RNA-protein complexesAnticodonRNA Processing Post-TranscriptionalUridine030304 developmental biologyAdaptor Proteins Signal TransducingAdenosine Triphosphatases0303 health sciencesSelenocysteineRNATRNA bindingCell biologychemistryTransfer RNASelenocysteine incorporationCarrier ProteinsRibosomes030217 neurology & neurosurgery
researchProduct

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
researchProduct

Analysis of involvement of the 3?-untranslated regions in regulating mRNA stability for vitellogenin, cyanoprotein ?, and cyanoprotein ? from the bea…

2002

The degradation of the 3'-untranslated regions (UTRs) of vitellogenin, cyanoprotein alpha, and cyanoprotein beta from the bean bug, Riptortus clavatus, was analyzed in vitro. The degradation pattern was similar for all three RNAs, with a high degradation rate in non-diapausing adult insects and no degradation in the fifth instar nymphs and in diapausing adults, and was not correlated with the expression levels of these three proteins. Proteins binding to the 3'-UTRs were detected in polysomal and cytosolic extracts. These factors, however, were present in all developmental stages. The abundance of the polysomal factor showed little variation, but the cytosolic factor was enriched in adult i…

Untranslated regionPhysiologyMolecular Sequence DatahexamerinElectrophoretic Mobility Shift AssayRNA-binding proteinBinding CompetitiveBiochemistryHemipteraVitellogeninsVitellogeninBotanyAnimalsRNA Messenger3' Untranslated RegionsRegulation of gene expressionMessenger RNABase Sequencebiologyjuvenile hormoneThree prime untranslated regionRNA-Binding ProteinsRNAGeneral MedicineRNA binding proteincyanoproteindiapauseGene Expression RegulationBiochemistryInsect ScienceJuvenile hormonebiology.proteinInsect ProteinsSequence AlignmentArchives of Insect Biochemistry and Physiology
researchProduct

Polycationic Monomeric and Homodimeric Asymmetric Monomethine Cyanine Dyes with Hydroxypropyl Functionality—Strong Affinity Nucleic Acids Binders

2021

New analogs of the commercial asymmetric monomethine cyanine dyes thiazole orange (TO) and thiazole orange homodimer (TOTO) with hydroxypropyl functionality were synthesized and their properties in the presence of different nucleic acids were studied. The novel compounds showed strong, micromolar and submicromolar affinities to all examined DNA ds-polynucleotides and poly rA–poly rU. The compounds studied showed selectivity towards GC-DNA base pairs over AT-DNA, which included both binding affinity and a strong fluorescence response. CD titrations showed aggregation along the polynucleotide with well-defined supramolecular chirality. The single dipyridinium-bridged dimer showed intercalatio…

antiproliferative activityCircular dichroismSupramolecular chiralityDimerIntercalation (chemistry)cyanine dye010402 general chemistry01 natural sciencesBiochemistryMicrobiologyArticlechemistry.chemical_compoundCell Line TumorHumansCyanineDNA bindingColoring AgentsBiologyMolecular BiologyBinding Sites010405 organic chemistrycyanine dye ; DNA binding ; RNA binding ; fluorescence ; circular dichroism ; antiproliferative activityDNARNA bindingCombinatorial chemistryQR1-502Intercalating Agents3. Good health0104 chemical sciencescircular dichroismchemistryPolynucleotideNucleic acidcyanine dye; DNA binding; RNA binding; fluorescence; circular dichroism; antiproliferative activityfluorescenceDNA
researchProduct