Search results for "binding"

showing 10 items of 3896 documents

Comparison of DNase, DNA-polymerase and RNA-polymerase activities present in the DNA-bindung proteins of normal human dermis, epidermis, horny layer …

1978

DNA-binding proteins (DBP) of normal human dermis, epidermis, horny layer and psoriatic scales represent a tissue-specific group of mostly nuclear nonhistone proteins. To analyse their function, the different DBP fractions were examined concerning the presence of DNase, DNA-polymerase and RNA-polymerase activities. DBP of normal epidermis and horny layer contain four different DNases. One DNase of both DBP fractions is active only at pH 5.0. Three DNases of epidermal DBP are active at a pH-range from 5.0--8.5, while the corresponding DNases of horny layer-DBP are most active at pH 7.4. Probably these DNases have changed their pH-optimum during keratinisation. DBP of psoriatic scales include…

DNA polymeraseDNA-Directed DNA PolymeraseDermatologychemistry.chemical_compoundNon-histone proteinDermisRNA polymerasemedicineHumansPsoriasisSkinchemistry.chemical_classificationThymidine monophosphateDeoxyribonucleasesEpidermis (botany)biologyIsoelectric focusingProteinsDNA-Directed RNA PolymerasesGeneral MedicineElectrophoresis DiscMolecular biologyEnzyme Activationmedicine.anatomical_structureEnzymechemistrybiology.proteinEpidermisIsoelectric FocusingProtein Bindingcirculatory and respiratory physiologyArchives of Dermatological Research
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Mutations in CTC1, encoding conserved telomere maintenance component 1, cause Coats plus

2012

Coats plus is a highly pleiotropic disorder particularly affecting the eye, brain, bone and gastrointestinal tract. Here, we show that Coats plus results from mutations in CTC1, encoding conserved telomere maintenance component 1, a member of the mammalian homolog of the yeast heterotrimeric CST telomeric capping complex. Consistent with the observation of shortened telomeres in an Arabidopsis CTC1 mutant and the phenotypic overlap of Coats plus with the telomeric maintenance disorders comprising dyskeratosis congenita, we observed shortened telomeres in three individuals with Coats plus and an increase in spontaneous γ 3H2AX-positive cells in cell lines derived from two affected individual…

DNA polymeraseMolecular Sequence DataTelomere-Binding ProteinsHistones/metabolismHDE GENHDE NEU PEDCST complexCEREBRORETINAL MICROANGIOPATHY FAMILIAL SYNDROME CALCIFICATIONS CYSTS PROTEIN DNA LEUKOENCEPHALOPATHY EVOLUTION DEFECTSHistoneschemistry.chemical_compoundAbnormalities Multiple/geneticsGeneticsmedicineAbnormalities MultipleGenetic Predisposition to DiseaseGeneticsTelomere-binding proteinTelomere/pathologyddc:618biologyBase SequenceGenetic Predisposition to Disease/geneticsDNA replicationSequence Analysis DNATelomeremedicine.diseaseFlow CytometryTelomereCell biologyRetinal Telangiectasis/genetics/pathologychemistrySequence Analysis DNA/methodsbiology.proteinRetinal TelangiectasisPrimaseTelomere-Binding Proteins/geneticsDNADyskeratosis congenitaNature Genetics
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Cloning, deletion, and characterization of PadR, the transcriptional repressor of the phenolic acid decarboxylase-encoding padA gene of Lactobacillus…

2004

ABSTRACTLactobacillus plantarumdisplays a substrate-induciblepadAgene encoding a phenolic acid decarboxylase enzyme (PadA) that is considered a specific chemical stress response to the inducing substrate. The putative regulator ofpadAwas located in thepadAlocus based on its 52% identity with PadR, thepadAgene transcriptional regulator ofPediococcus pentosaceus(L. Barthelmebs, B. Lecomte, C. Diviès, and J.-F. Cavin, J. Bacteriol.182:6724-6731, 2000). Deletion of theL. plantarum padRgene clearly demonstrates that the protein it encodes is the transcriptional repressor of divergently orientedpadA. ThepadRgene is cotranscribed with a downstream open reading frame (ORF1), the product of which m…

DNA BacterialCoumaric AcidsCarboxy-LyasesMolecular Sequence DataRepressorGenetics and Molecular BiologyBiologymedicine.disease_causeApplied Microbiology and BiotechnologyOpen Reading FramesBacterial ProteinsTranscription (biology)Transcriptional regulationmedicineAmino Acid SequenceCloning MolecularPromoter Regions GeneticGeneEscherichia coliDNA PrimersBinding SitesEcologyBase SequenceSequence Homology Amino Acidfood and beveragesPromoterbiology.organism_classificationMolecular biologyRepressor ProteinsOpen reading frameLactobacillusBiochemistryGenes BacterialPropionatesLactobacillus plantarumGene DeletionFood ScienceBiotechnologyApplied and environmental microbiology
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Efficient Control of raf Gene Expression by CAP and Two Raf Repressors that Bend DNA in Opposite Directions

1999

The plasmid-borne raf operon of Escherichia coli encodes proteins involved in the uptake and utilisation of the trisaccharide raffinose. The operon is subject to dual regulation; to negative control by the binding of RafR repressor to twin operators, O1 and O2, and to positive control by the cAMP-binding protein, CAP. We have identified the CAP binding site (CBS) as a 22 bp palindromic sequence with incomplete dyad symmetry by deletion analysis, DNasel footprinting and electrophoretic mobility shift assays (EMSA) of CAP-DNA complexes. The CBS is centred 60.5 bp upstream of the transcription start point and partially overlaps O1. In vivo, CAP increases rafA (alpha-galactosidase) gene express…

DNA BacterialCyclic AMP Receptor ProteinOperonMolecular Sequence DataClinical BiochemistryRepressorCooperativityBiologyBiochemistrychemistry.chemical_compoundBacterial ProteinsGene expressionCyclic AMPBinding siteMolecular BiologyDyad symmetryPalindromic sequenceBinding SitesBase SequenceGene Expression Regulation BacterialMolecular biologyProto-Oncogene Proteins c-rafchemistryGenes BacterialNucleic Acid ConformationCarrier ProteinsDNABiological Chemistry
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Growth phase-dependent regulation of nuoA-N expression in Escherichia coli K-12 by the Fis protein: upstream binding sites and bioenergetic significa…

2000

The expression of the nuoA-N operon of Escherichia coli K-12, which encodes the proton-pumping NADH dehydrogenase I is modulated by growth phase-dependent regulation. Under respiratory growth conditions, expression was stimulated in early exponential, and to a lesser extent in late exponential and stationary growth phases. The stimulation in the early exponential growth phase was not observed in fis mutants, which are deficient for the growth phase-responsive regulator Fis. Neither the alternative sigma factor RpoS nor the integration host factor (IHF) are involved in growth phase-dependent regulation of this operon. When incubated with nuo promoter DNA, isolated Fis protein formed three re…

DNA BacterialIntegration Host FactorsOperonMutantMolecular Sequence DataBiologymedicine.disease_causeExponential growthBacterial ProteinsFactor For Inversion Stimulation ProteinOperonGeneticsmedicineEscherichia coliBinding sitePromoter Regions GeneticMolecular BiologyEscherichia coliBinding SitesBase SequenceEscherichia coli ProteinsDNase-I FootprintingPromoterMolecular biologyCarrier ProteinsrpoSMoleculargeneral genetics : MGG
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Requirement of the Lactobacillus casei MaeKR two-component system for L-malic acid utilization via a malic enzyme pathway.

2009

ABSTRACTLactobacillus caseican metabolizel-malic acid via malolactic enzyme (malolactic fermentation [MLF]) or malic enzyme (ME). Whereas utilization ofl-malic acid via MLF does not support growth, the ME pathway enablesL. caseito grow onl-malic acid. In this work, we have identified in the genomes ofL. caseistrains BL23 and ATCC 334 a cluster consisting of two diverging operons,maePEandmaeKR, encoding a putative malate transporter (maeP), an ME (maeE), and a two-component (TC) system belonging to the citrate family (maeKandmaeR). Homologous clusters were identified inEnterococcus faecalis,Streptococcus agalactiae,Streptococcus pyogenes, andStreptococcus uberis. Our results show that ME is …

DNA BacterialLactobacillus caseiHistidine KinaseMalic enzymeCatabolite repressionDNA FootprintingMalatesGenetics and Molecular Biologymedicine.disease_causeApplied Microbiology and Biotechnologychemistry.chemical_compoundBacterial ProteinsOperonmedicineEnterococcus faecalisDirect repeatPromoter Regions Geneticchemistry.chemical_classificationEcologybiologySequence Homology Amino AcidGene Expression Profilingfungifood and beveragesStreptococcusGene Expression Regulation Bacterialbiology.organism_classificationMolecular biologyAmino acidResponse regulatorLacticaseibacillus caseichemistryBiochemistryMultigene FamilyStreptococcus pyogenesMalic acidProtein KinasesMetabolic Networks and PathwaysFood ScienceBiotechnologyProtein BindingSignal TransductionTranscription FactorsApplied and environmental microbiology
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Role of two operators in regulating the plasmid-borne raf operon of Escherichia coli

1994

The plasmid-borne raf operon encodes functions required for the inducible uptake and utilization of raffinose in Escherichia coli K12. The expression of three structural genes for alpha-galactosidase (rafA), Raf permease (rafB) and sucrose hydrolase (rafD) is negatively controlled by the binding of RafR repressor (rafR) to two operator sites, O1 and O2, that flank the -35 sequence of the raf promoter, PA. In vitro, O1 and O2 are occupied on increasing the concentration of RafR, without detectable preference for one site or the other or any indication of cooperative binding. Nucleotide substitutions at positions 3, 4 or 5 in an operator half-site prevented repressor binding, supporting a mod…

DNA BacterialOperator Regions GeneticOperonBase pairMolecular Sequence DataRepressorBiologyBinding CompetitiveRaffinoseTranscription (biology)OperonEscherichia coliGeneticsBinding siteSite-directed mutagenesisMolecular BiologyBase SequenceHelix-Loop-Helix MotifsStructural geneCooperative bindingGene Expression Regulation BacterialDNA-Binding ProteinsRepressor ProteinsBiochemistryGenes Bacterialalpha-GalactosidaseMutagenesis Site-DirectedAutoradiographyElectrophoresis Polyacrylamide GelPlasmidsMolecular and General Genetics MGG
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Prephenate dehydratase from the aphid endosymbiont (Buchnera) displays changes in the regulatory domain that suggest its desensitization to inhibitio…

2000

ABSTRACT Buchnera aphidicola , the prokaryotic endosymbiont of aphids, complements dietary deficiencies with the synthesis and provision of several essential amino acids. We have cloned and sequenced a region of the genome of B. aphidicola isolated from Acyrthosiphon pisum which includes the two-domain aroQ/pheA gene. This gene encodes the bifunctional chorismate mutase-prephenate dehydratase protein, which plays a central role in l -phenylalanine biosynthesis. Two changes involved in the overproduction of this amino acid have been detected. First, the absence of an attenuator region suggests a constitutive expression of this gene. Second, the regulatory domain of the Buchnera prephenate de…

DNA BacterialPhenylalanineMolecular Sequence DataPrephenate dehydratasePhenylalanineMicrobiologychemistry.chemical_compoundBiosynthesisBuchneraEscherichia coliAnimalsHumansAmino Acid SequenceEnzyme InhibitorsSymbiosisMolecular BiologyGenechemistry.chemical_classificationGeneticsBinding SitesbiologyBase SequenceSequence Homology Amino Acidbiochemical phenomena metabolism and nutritionbiology.organism_classificationPrephenate DehydrataseAmino acidEnzymeBiochemistrychemistryDehydrataseAphidsBuchneraGenome BacterialPopulation Genetics and EvolutionChorismate MutaseJournal of bacteriology
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Multiple Site-Specific Binding of Fis Protein to Escherichia coli nuoA-N Promoter DNA and its Impact on DNA Topology Visualised by Means of Scanning …

2004

DNA BacterialPlasma protein bindingMicroscopy Atomic Forcemedicine.disease_causeBiochemistryBacterial geneticsMitochondrial Proteinschemistry.chemical_compoundScanning probe microscopyMicroscopyEscherichia coliImage Processing Computer-AssistedmedicinePromoter Regions GeneticMolecular BiologyEscherichia coliDNA PrimersReverse Transcriptase Polymerase Chain ReactionOrganic ChemistryMembrane ProteinsPromoterMolecular biologyMembrane proteinchemistryMolecular MedicineDNAProtein BindingChemBioChem
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Influence of molecular weight of DNA on the determination of anti-DNA antibodies in systemic lupus erythematosus (SLE) sera by radioimmunoassay

1975

Using a radioimmunoassay (RIA) based on the Farr technique with radioactively labeled 3-H-DNA for quantitative measurements of anti-DNA antibodies in sera of patients with systemic lupus erythematosus (SLE), the influence of molecular weight of DNA (ranging from 0.1 times 10-6 to 22.0 times 10-6 daltons) on binding and precipitation in this system has been investigated. Comparing our results with mathematical models it follows that one antibody molecule is fixed on the average to a statistical DNA segment of 2 times 10-6 to 4 times 10-6 daltons. Furthermore binding capacity of the DNA was found to be independent of the molecular weight, as demonstrated in a double label experiment using 14-…

DNA BacterialRadioimmunoassayBiologyModels BiologicalAntibodieschemistry.chemical_compoundGeneticsmedicineChemical PrecipitationLupus Erythematosus SystemicBinding siteAnti dnaLupus erythematosusMolecular massRadioimmunoassayDNAmedicine.diseaseMolecular biologyMolecular WeightAntibody moleculechemistryBiochemistrybiology.proteinBinding Sites AntibodyAntibodyDNANucleic Acids Research
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