Search results for "carrier"

showing 10 items of 1256 documents

DAZAP2 acts as specifier of the p53 response to DNA damage.

2021

Abstract The DNA damage-responsive tumor suppressors p53 and HIPK2 are well established regulators of cell fate decision-making and regulate the cellular sensitivity to DNA-damaging drugs. Here, we identify Deleted in Azoospermia-associated protein 2 (DAZAP2), a small adaptor protein, as a novel regulator of HIPK2 and specifier of the DNA damage-induced p53 response. Knock-down or genetic deletion of DAZAP2 strongly potentiates cancer cell chemosensitivity both in cells and in vivo using a mouse tumour xenograft model. In unstressed cells, DAZAP2 stimulates HIPK2 polyubiquitination and degradation through interplay with the ubiquitin ligase SIAH1. Upon DNA damage, HIPK2 site-specifically ph…

DNA damageAcademicSubjects/SCI00010Ubiquitin-Protein LigasesRegulatorAntineoplastic AgentsCell fate determinationProtein Serine-Threonine Kinases03 medical and health sciencesMice0302 clinical medicineUbiquitinCell Line TumorGeneticsAnimalsPromoter Regions GeneticGeneMolecular BiologyCells Cultured030304 developmental biologyRegulation of gene expressionCell Nucleus0303 health sciencesbiologyNuclear ProteinsRNA-Binding ProteinsCell biologyUbiquitin ligaseGene Expression Regulation030220 oncology & carcinogenesisCancer cellbiology.proteinTumor Suppressor Protein p53Carrier ProteinsDNA DamageNucleic acids research
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Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster

1998

ABSTRACT A citrate lyase (EC 4.1.3.6 ) was purified 25-fold from Leuconostoc mesenteroides and was shown to contain three subunits. The first 42 amino acids of the β subunit were identified, as well as an internal peptide sequence spanning some 20 amino acids into the α subunit. Using degenerated primers from these sequences, we amplified a 1.2-kb DNA fragment by PCR from Leuconostoc mesenteroides subsp. cremoris . This fragment was used as a probe for screening a Leuconostoc genomic bank to identify the structural genes. The 2.7-kb gene cluster encoding citrate lyase of L. mesenteroides is organized in three open reading frames, citD , citE , and citF , encoding, respectively, the three ci…

DNA BacterialATP citrate lyaseMolecular Sequence DataGene ExpressionBiologymedicine.disease_causeMicrobiologyBacterial ProteinsCarbon-Sulfur LigasesMultienzyme ComplexesGene clusterAcyl Carrier ProteinEscherichia colimedicineLeuconostocAmino Acid SequenceCloning MolecularMolecular BiologyEscherichia coliBase SequenceSequence Homology Amino AcidStructural geneOxo-Acid-LyasesSequence Analysis DNALyasebiology.organism_classificationEnzymes and ProteinsMolecular biologyOxaloacetate decarboxylaseBiochemistryGenes BacterialLeuconostoc mesenteroidesMultigene FamilyCoenzyme A-TransferasesLeuconostoc
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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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Virulence and Molecular Typing of Vibrio harveyi Strains Isolated from Cultured Dentex, Gilthead Sea Bream and European Sea Bass

2003

Vibrio harveyi was isolated from internal organs or ulcers of diseased and apparently healthy gilthead sea bream (Sparus aurata) and European sea bass (Dicentrarchus labrax) cultured in several fish farms located on the Spanish Mediterranean coast. The prevalence of the bacterium was significantly higher in European sea bass than in gilthead sea bream, and was closely related to the season in both fish species, occurring almost exclusively on warm months (June to November). After phenotypic characterization, a selection of forty five isolates from gilthead sea bream, sea bass, and several isolates previously obtained from common dentex (Dentex dentex) of the same area, were molecularly type…

DNA BacterialFish farmingFisheriesVirulenceZoologyMediterranean aquacultureRibotypingApplied Microbiology and BiotechnologyMicrobiologyFish DiseasesRibotypingRAPDSparus aurataAnimalsDicentrarchus labraxSea bassFish pathogensEcology Evolution Behavior and SystematicsVibrioVirulencebiologyVibrio harveyiLD50Dentex dentexbiology.organism_classificationVibrio harveyiSea BreamBacterial Typing TechniquesPerciformesRandom Amplified Polymorphic DNA TechniqueRAPDFisheryPhenotypeVibrio InfectionsCarrier StateBassDicentrarchussense organsDentex dentexSystematic and Applied Microbiology
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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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Identification of a third secondary carrier (DcuC) for anaerobic C4-dicarboxylate transport in Escherichia coli: roles of the three Dcu carriers in u…

1996

In Escherichia coli, two carriers (DcuA and DcuB) for the transport of C4 dicarboxylates in anaerobic growth were known. Here a novel gene dcuC was identified encoding a secondary carrier (DcuC) for C4 dicarboxylates which is functional in anaerobic growth. The dcuC gene is located at min 14.1 of the E. coli map in the counterclockwise orientation. The dcuC gene combines two open reading frames found in other strains of E. coli K-12. The gene product (DcuC) is responsible for the transport of C4 dicarboxylates in DcuA-DcuB-deficient cells. The triple mutant (dcuA dcuB dcuC) is completely devoid of C4-dicarboxylate transport (exchange and uptake) during anaerobic growth, and the bacteria are…

DNA BacterialMutantMolecular Sequence DataBiologymedicine.disease_causeMicrobiologyGene productBacterial ProteinsmedicineEscherichia coliDicarboxylic AcidsAmino Acid SequenceAnaerobiosisMolecular BiologyEscherichia coliPeptide sequenceGeneDicarboxylic Acid TransportersBase SequenceSequence Homology Amino AcidEscherichia coli ProteinsChromosome MappingBiological Transportbiology.organism_classificationIsoenzymesOpen reading frameMutagenesis InsertionalBiochemistryC4-dicarboxylate transportCarrier ProteinsBacteriaResearch ArticleJournal of bacteriology
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The long-term cytoskeletal rearrangement induced by rabbit enteropathogenic Escherichia coli is Esp dependent but intimin independent.

1999

Attaching and effacing rabbit enteropathogenic Escherichia coli (REPEC) of the O103 serogroup adhere diffusely on HeLa cells and trigger a slow progressive cytopathic effect (CPE) characterized by the recruitment of vinculin and the assembly of actin stress fibres. In contrast to REPEC O103, the reference human EPEC strain E2348/69 is unable to trigger the CPE. In this study, we have shown first that the fimbrial adhesin AF/R2, which mediates the diffuse adhesion of REPEC O103, was not sufficient to induce the CPE capability upon E2348/69. Non-polar mutants of REPEC O103 for espA, espB, espD and eae were then constructed. The four mutants were unable to induce attaching and effacing lesions…

DNA BacterialMutantMolecular Sequence DataMicrobiologyBacterial AdhesionMicrobiology03 medical and health sciencesBacterial ProteinsEscherichia coliAnimalsHumansEnteropathogenic Escherichia coliCytoskeletonAdhesins BacterialMolecular Biology[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyActinCytoskeleton030304 developmental biologyIntiminCytopathic effect0303 health sciencesAdhesins Escherichia colibiologyBase Sequence030306 microbiologyEscherichia coli ProteinsGenetic Complementation TestREARRANGEMENTbiochemical phenomena metabolism and nutritionVinculinBacterial adhesin[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyGenes Bacterialbiology.proteinRabbitsCarrier ProteinsBacterial Outer Membrane ProteinsHeLa CellsMolecular microbiology
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Myosin VIIa, harmonin and cadherin 23, three Usher I gene products that cooperate to shape the sensory hair cell bundle

2002

Deaf-blindness in three distinct genetic forms of Usher type I syndrome (USH1) is caused by defects in myosin VIIa, harmonin and cadherin 23. Despite being critical for hearing, the functions of these proteins in the inner ear remain elusive. Here we show that harmonin, a PDZ domain-containing protein, and cadherin 23 are both present in the growing stereocilia and that they bind to each other. Moreover, we demonstrate that harmonin b is an F-actin-bundling protein, which is thus likely to anchor cadherin 23 to the stereocilia microfilaments, thereby identifying a novel anchorage mode of the cadherins to the actin cytoskeleton. Moreover, harmonin b interacts directly with myosin VIIa, and i…

DNA ComplementaryCadherin Related ProteinsCell Cycle Proteinsmacromolecular substancesMyosinsBiologyTransfectionMicrofilamentGeneral Biochemistry Genetics and Molecular BiologyCell LineMiceCDH23Two-Hybrid System TechniquesHair Cells Auditoryotorhinolaryngologic diseasesmedicineAnimalsHumansProtein IsoformsRats WistarMolecular BiologyActinAdaptor Proteins Signal TransducingGene LibraryGeneral Immunology and MicrobiologyCadherinGeneral NeuroscienceStereociliaDyneinsCell DifferentiationArticlesCadherinsActin cytoskeletonActinsProtein Structure TertiaryRatsCell biologyCytoskeletal ProteinsMicroscopy Electronmedicine.anatomical_structureMicroscopy FluorescenceMyosin VIIasense organsCarrier ProteinsTip linkPCDH15HeLa CellsProtein BindingThe EMBO Journal
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Key Disulfide Bonds in an Insect Hormone Binding Protein: cDNA Cloning of a Juvenile Hormone Binding Protein of Heliothis virescens and Ligand Bindin…

1995

The hemolymph juvenile hormone binding protein (JHBP) from the early fifth instar larvae of Heliothis virescens (Lepidoptera, Noctuidae) has been purified, and three cDNA clones for this protein have been isolated from a fat body cDNA library constructed in bacteriophage λZAP XR. The deduced amino acid sequence of the full-length clone predicts a mature protein consisting of 224 residues, a molecular mass of 24 976 Da, and a p/ of 5.29. Comparison of the amino acid sequence to that of the previously described JHBP from Manduca sexta shows 51 % overall identity with highly conserved N- and C-terminal regions. One of the three clones bound photoactivatable analogs of juvenile hormones with mu…

DNA ComplementaryPhotochemistryphenylalanineMolecular Sequence DataMutantcomplementary DNAMothsBiochemistryHemolymphComplementary DNAAnimalsAmino Acid SequenceDisulfidesCloning MolecularcysteinePeptide sequencehormone binding proteinhormone analogHormone binding proteinBase SequencePhotoaffinity labelingMolecular massjuvenile hormoneChemistrycDNA libraryAffinity LabelsMolecular biologyJuvenile HormonesBiochemistryLarvaJuvenile hormoneMutagenesis Site-DirectedInsect ProteinsalanineCarrier ProteinsBiochemistry
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Size dependent carrier thermal escape and transfer in bimodally distributed self assembled InAs/GaAs quantum dots

2012

We have investigated the temperature dependent recombination dynamics in two bimodally distributed InAs self assembled quantum dots samples. A rate equations model has been implemented to investigate the thermally activated carrier escape mechanism which changes from exciton-like to uncorrelated electron and hole pairs as the quantum dot size varies. For the smaller dots, we find a hot exciton thermal escape process. We evaluated the thermal transfer process between quantum dots by the quantum dot density and carrier escape properties of both samples. © 2012 American Institute of Physics.

DYNAMICSMaterials scienceAtmospheric escapeCondensed matter physicsExcitonGeneral Physics and AstronomyElectronRate equationThermal transferEPITAXYCondensed Matter::Mesoscopic Systems and Quantum Hall EffectGallium arsenidechemistry.chemical_compoundCondensed Matter::Materials SciencechemistrySTATESself assembled quantum dots rate equations model carrier escape propertiesQuantum dotQuantum dot laserLUMINESCENCEPHOTOLUMINESCENCE
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