Search results for "Exonuclease"

showing 10 items of 11 documents

The exonuclease Xrn1 activates transcription and translation of mRNAs encoding membrane proteins

2019

The highly conserved 5’–3’ exonuclease Xrn1 regulates gene expression in eukaryotes by coupling nuclear DNA transcription to cytosolic mRNA decay. By integrating transcriptome-wide analyses of translation with biochemical and functional studies, we demonstrate an unanticipated regulatory role of Xrn1 in protein synthesis. Xrn1 promotes translation of a specific group of transcripts encoding membrane proteins. Xrn1-dependence for translation is linked to poor structural RNA contexts for translation initiation, is mediated by interactions with components of the translation initiation machinery and correlates with an Xrn1-dependence for mRNA localization at the endoplasmic reticulum, the trans…

0301 basic medicineExonucleaseCell biologySaccharomyces cerevisiae ProteinsTranscription GeneticMolecular biologyScienceRNA StabilityGenetic VectorsGeneral Physics and AstronomyGene Expression02 engineering and technologySaccharomyces cerevisiaeEndoplasmic ReticulumGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesEukaryotic translationTranscription (biology)Gene Expression Regulation FungalGene expression540 ChemistryProtein biosynthesisRNA MessengerCloning Molecularlcsh:ScienceRegulation of gene expressionMultidisciplinarybiologyChemistryGene Expression ProfilingQMembrane ProteinsTranslation (biology)General Chemistry021001 nanoscience & nanotechnologyRibosomeRecombinant Proteins3. Good healthCell biology030104 developmental biologyMembrane proteinProtein BiosynthesisExoribonucleasesbiology.protein570 Life sciences; biologylcsh:Q0210 nano-technologySignal Transduction
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iDamIDseq and iDEAR: an improved method and computational pipeline to profile chromatin-binding proteins

2016

DNA adenine methyltransferase identification (DamID) has emerged as an alternative method to profile protein-DNA interactions; however, critical issues limit its widespread applicability. Here, we present iDamIDseq, a protocol that improves specificity and sensitivity by inverting the steps DpnI-DpnII and adding steps that involve a phosphatase and exonuclease. To determine genome-wide protein-DNA interactions efficiently, we present the analysis tool iDEAR (iDamIDseq Enrichment Analysis with R). The combination of DamID and iDEAR permits the establishment of consistent profiles for transcription factors, even in transient assays, as we exemplify using the small teleost medaka (Oryzias lati…

0301 basic medicineExonucleaseSite-Specific DNA-Methyltransferase (Adenine-Specific)Embryo NonmammalianOryziasOryziasComputational biologyBiology03 medical and health scienceschemistry.chemical_compoundTechniques and ResourcesTranscriptional regulationDatabases GeneticProtein Interaction MappingTranscriptional regulationAnimalsEpigeneticsPromoter Regions GeneticMolecular BiologyTranscription factorGeneticsBinding SitesChromatin bindingComputational BiologyPromoterSequence Analysis DNADNA Methylationbiology.organism_classificationChromatinDNA-Binding Proteins030104 developmental biologychemistryGene Expression Regulation207Chromatin profilingbiology.proteinDamIDEpigeneticsTranscription factorDNAAlgorithmsDevelopmental BiologyProtein BindingTranscription FactorsDevelopment (Cambridge, England)
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DNA oxidation products determined with repair endonucleases in mammalian cells: Types, basal levels and influence of cell proliferation

1999

Purified repair endonucleases such as Fpg protein, endonuclease III and IV allow a very sensitive quantification of various types of oxidative DNA modifications in mammalian cells. By means of these assays, the numbers of base modifications sensitive to Fpg protein, which include 8-hydroxyguanine (8-oxoG), were determined to be less than 0.3 per 10(6) bp in several types of untreated cultured mammalian cells and human lymphocytes and less than 10 per 10(6) bp in mitochondrial DNA from rat and porcine liver. Oxidative 5,6-dihydropyrimidine derivatives sensitive to endonuclease III and sites of base loss sensitive to endonuclease IV or exonuclease III were much less frequent than Fpg-sensitiv…

DNA RepairBase pairDNA repairDNA damageCarbon-Oxygen LyasesCHO CellsDeferoxamineBiochemistryDeoxyribonuclease (Pyrimidine Dimer)chemistry.chemical_compoundCricetinaeDNA-(Apurinic or Apyrimidinic Site) LyaseAnimalsHumansDimethyl SulfoxideBase PairingN-Glycosyl HydrolasesChromatography High Pressure LiquidMammalsExonuclease IIIEndodeoxyribonucleasesPhotosensitizing AgentsGuanosinebiologyEscherichia coli ProteinsAcridine orangeDNAGeneral MedicineDNA oxidationOxidantsMolecular biologyDNA-(apurinic or apyrimidinic site) lyaseDeoxyribonuclease IV (Phage T4-Induced)DNA-Formamidopyrimidine GlycosylasechemistryBiochemistrybiology.proteinOxidation-ReductionCell DivisionDNAHeLa CellsFree Radical Research
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DNA damage by peroxynitrite characterized with DNA repair enzymes.

1996

The DNA damage induced by peroxynitrite in isolated bacteriophage PM2 DNA was characterized by means of several repair enzymes with defined substrate specificities. Similar results were obtained with peroxynitrite itself and with 3-morpholinosydnonimine (SIN-1), a compound generating the precursors of peroxynitrite, nitric oxide and superoxide. A high number of base modifications sensitive to Fpg protein which, according to HPLC analysis, were mostly 8-hydroxyguanine residues, and half as many single-strand breaks were observed, while the numbers of oxidized pyrimidines (sensitive to endonuclease III) and of sites of base loss (sensitive to exonuclease III or T4 endonuclease V) were relativ…

DNA Repairtert-Butyl AlcoholDNA repairDNA damageRadicalButanolsEndonucleasechemistry.chemical_compoundGeneticsChromatography High Pressure LiquidExonuclease IIINitratesbiologyHydroxyl RadicalDNAFree Radical ScavengersEndonucleasesBiochemistrychemistryMolsidominebiology.proteinHydroxyl radicalDNAPeroxynitriteResearch ArticleDNA Damage
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Sequential recruitment of the mRNA decay machinery to the iron-regulated protein Cth2 in Saccharomyces cerevisiae

2020

Post-transcriptional factors importantly contribute to the rapid and coordinated expression of the multiple genes required for the adaptation of living organisms to environmental stresses. In the model eukaryote Saccharomyces cerevisiae, a conserved mRNA-binding protein, known as Cth2, modulates the metabolic response to iron deficiency. Cth2 is a tandem zinc-finger (TZF)-containing protein that co-transcriptionally binds to adenine/uracil-rich elements (ARE) present in the 3′-untranslated region of iron-related mRNAs to promote their turnover. The nuclear binding of Cth2 to mRNAs via its TZFs is indispensable for its export to the cytoplasm. Although Cth2 nucleocytoplasmic transport is ess…

Exonuclease:YeastSaccharomyces cerevisiae ProteinsIronRNA StabilitySaccharomyces cerevisiaeAdaptation BiologicalBiophysicsSaccharomyces cerevisiaeBiochemistryDEAD-box RNA Helicases03 medical and health sciencesTristetraprolinStructural BiologyGene Expression Regulation FungalGene expressionGenetics[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyRNA MessengerMolecular BiologyPost-transcriptional regulationGene030304 developmental biology0303 health sciencesbiologyChemistryPost-transcriptional regulationIron deficiency030302 biochemistry & molecular biologyIron-Regulatory ProteinsIron Deficienciesbiology.organism_classificationRNA Helicase AYeast3. Good healthCell biology[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsCytoplasmbiology.proteinGene expressionFunction (biology)
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Neutral deoxyribonucleases of HeLa S3 cells: electrophoretic separation, characterization, substrate specificity and mode of action.

1980

Extracts of HeLa S3 cells were electrophoresed on polyacrylamide gels; gel slices were eluted and the eluates were assayed for DNase activities against native and denatured DNA substrates in the presence of MgCl2 or Na2EDTA. Aliquots of each eluate were also assayed for their ability to nick the circular supercoiled PM2 phage DNA to distinguish endonucleases from exonucleases. Peaks of endonuclease activities were characterized as forming 3′-phospho-oligonucleotides or 5′-phospho-oligonucleotides by the use of oligonucleotides produced by these enzymes as substrates for the 5′-phosphate-specific snake venom exonuclease. The total activity of DNases in gel eluates was much higher than that i…

ExonucleasePolyacrylamideDNA Single-StrandedBiochemistrySubstrate SpecificityEndonucleasechemistry.chemical_compoundHumansMagnesiumEdetic Acidchemistry.chemical_classificationChromatographyDeoxyribonucleasesbiologyOligonucleotideHydrogen-Ion ConcentrationElectrophoresisEnzymeBiochemistrychemistryDNA Viralbiology.proteinElectrophoresis Polyacrylamide GelDNA CircularDeoxyribonucleasesDNAHeLa CellsEuropean journal of biochemistry
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Control of Enzymic Hydrolysis of Polyadenylate Segment of Messenger RNA: Role of Polyadenylate-Associated Proteins

1978

The role of poly(A)-associated proteins in the breakdown of poly(A) sequences in both mammalian polyribosomes and in isolated poly(A) · protein complexes has been studied on an enzymic level. Two nucleases (alkaline exoribonuclease and endoribonuclease IV; both isolated from eukaryotic tissue), which preferentially hydrolyze poly(A) sequences, have been applied to determine the susceptibility of poly(A) in dependence on the presence of poly(A) · protein(s). Polysomes, isolated from L5178y mouse lymphoma cells, do not contain endogenous poly(A) nuclease activity. The poly(A) segment in polysomes is hydrolyzed by the exoribonuclease, irrespective of the preincubation conditions used. Pretreat…

Exonucleaseschemistry.chemical_classificationNucleaseMessenger RNAbiologyEndonucleasesBiochemistryMolecular biologyCell LineKineticschemistry.chemical_compoundNucleoproteinsRibonucleasesEnzymechemistryBiochemistryPolyribosomesExoribonucleasePolysomebiology.proteinUreaPolyadenylateRNA MessengerRibonucleasePoly AEuropean Journal of Biochemistry
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Photolysis of N-hydroxpyridinethiones: a new source of hydroxyl radicals for the direct damage of cell-free and cellular DNA.

1996

N-Hydroxypyridine-2-thione (2-HPT), known to release hydroxyl radicals on irradiation with visible light, and two related compounds, viz. N-hydroxypyridine-4-thione (4-HPT) and N-hydroxyacridine-9-thione (HAT), were tested for their potency to induce DNA damage in L1210 mouse leukemia cells and in isolated DNA from bacteriophage PM2. DNA single-strand breaks and modifications sensitive to various repair endonucleases (Fpg protein, endonuclease III, exonuclease III, T4 endonuclease V) were quantified. Illumination of cell-free DNA in the presence of 2-HPT and 4-HPT gave rise to damage profiles characteristic for hydroxyl radicals, i.e. single-strand breaks and the various endonuclease-sensit…

LightDNA damageCell SurvivalPyridinesRadicalFree radical damage to DNABiologychemistry.chemical_compoundEndonucleaseMiceSuperoxidesGeneticsTumor Cells CulturedAnimalsBacteriophagesLeukemia L1210chemistry.chemical_classificationExonuclease IIIReactive oxygen speciesEndodeoxyribonucleasesPhotolysisSinglet OxygenHydroxyl RadicalThionesDNAOxygenBiochemistrychemistryBiophysicsbiology.proteinAcridinesHydroxyl radicalReactive Oxygen SpeciesDNAResearch ArticleDNA Damage
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Compromised nuclear envelope integrity drives TREX1-dependent DNA damage and tumor cell invasion

2021

Although mutations leading to a compromised nuclear envelope cause diseases such as muscular dystrophies or accelerated aging, the consequences of mechanically induced nuclear envelope ruptures are less known. Here, we show that nuclear envelope ruptures induce DNA damage that promotes senescence in non-transformed cells and induces an invasive phenotype in human breast cancer cells. We find that the endoplasmic reticulum (ER)-associated exonuclease TREX1 translocates into the nucleus after nuclear envelope rupture and is required to induce DNA damage. Inside the mammary duct, cellular crowding leads to nuclear envelope ruptures that generate TREX1-dependent DNA damage, thereby driving the …

SenescenceExonucleaseDNA damageNuclear Envelope[SDV]Life Sciences [q-bio]Breast NeoplasmsBiologySettore MED/08 - Anatomia PatologicaGeneral Biochemistry Genetics and Molecular BiologyCell LineMicemedicineSettore MED/05 - Patologia ClinicaAnimalsHumansNeoplasm InvasivenessEpithelial–mesenchymal transitionCellular SenescenceEndoplasmic reticulumPhosphoproteinsXenograft Model Antitumor AssaysCell biology[SDV] Life Sciences [q-bio]medicine.anatomical_structureExodeoxyribonucleasesCancer cellProteolysisbiology.proteinTREX1 nuclear envelope rupture DNA damage mammary duct carcinoma tumor invasion senescence breast cancer cGAS confinement epithelial to mesenchymal transition Animals Breast Neoplasms Cell Line Cellular Senescence Collagen Disease Progression Exodeoxyribonucleases Female Humans Mice Neoplasm InvasivenessNuclear Envelope PhosphoproteinsProteolysis Xenograft Model Antitumor Assays DNA DamageDisease ProgressionFemaleCollagenNucleusExtracellular Matrix DegradationDNA Damage
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Determination of steady-state levels of oxidative DNA base modifications in mammalian cells by means of repair endonucleases

1997

The alkaline elution technique in combination with various repair endonucleases (Fpg protein, endonuclease III, exonuclease III, T4 endonuclease V) was used to quantify steady-state (background) levels of oxidative base modifications in various types of mammalian cells. In human lymphocytes the number of base modifications sensitive to Fpg protein, which include 8-hydroxyguanine, was 0.25 +/- 0.05 per 10(6) base pairs. Even lower levels (0.07 +/- 0.02 per 10(6) bp) were observed in HeLa cells. The numbers of sites sensitive to the other repair endonucleases were below the detection limit (0.05 per 10(6) bp). In a direct comparison, the background level of Fpg-sensitive modifications determi…

chemistry.chemical_classificationExonuclease IIIExonucleaseCancer ResearchGuanineDNA RepairbiologyBase pairDNA repairDNAGeneral MedicineEndonucleasesMolecular biologyDNA extractionEndonucleasechemistry.chemical_compoundEnzymeBiochemistrychemistryElectrochemistrybiology.proteinHumansOxidation-ReductionChromatography High Pressure LiquidDNACarcinogenesis
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