Search results for " Site-Directed"

showing 10 items of 132 documents

Novel mutations of the MET proto-oncogene in papillary renal carcinomas.

1999

Hereditary papillary renal carcinoma (HPRC) is characterized by multiple, bilateral papillary renal carcinomas. Previously, we demonstrated missense mutations in the tyrosine kinase domain of the MET proto-oncogene in HPRC and a subset of sporadic papillary renal carcinomas. In this study, we screened a large panel of sporadic papillary renal carcinomas and various solid tumors for mutations in the MET proto-oncogene. Summarizing these and previous results, mutations of the MET proto-oncogene were detected in 17/129 sporadic papillary renal carcinomas but not in other solid tumors. We detected five novel missense mutations; three of five mutations were located in the ATP-binding region of t…

AdenomaModels MolecularCancer ResearchProtein ConformationDNA Mutational AnalysisMolecular Sequence DataHereditary Papillary Renal Cell CarcinomaBiologymedicine.disease_causeTransfectionProto-Oncogene MasReceptor tyrosine kinaseMiceAdenosine TriphosphateNeoplastic Syndromes HereditaryProto-OncogenesGeneticsCarcinomamedicineMissense mutationAnimalsHumansPoint MutationAmino Acid SequencePhosphorylationCodonMolecular BiologyKidneyMutationBinding SitesSequence Homology Amino AcidPoint mutation3T3 CellsDNA NeoplasmProto-Oncogene Proteins c-metmedicine.diseaseCarcinoma PapillaryKidney NeoplasmsNeoplasm Proteinsmedicine.anatomical_structureCell Transformation NeoplasticCancer researchbiology.proteinMutagenesis Site-DirectedTyrosine kinaseProtein Processing Post-TranslationalSequence AlignmentOncogene
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Na+ ions binding to the bradykinin B2 receptor suppress agonist-independent receptor activation.

1996

Control of the balance between receptor activation and inactivation is a prerequisite for seven transmembrane domain (7TM) receptor function. We asked for a mechanism to stabilize the inactive receptor conformation which prevents agonist-independent receptor activation. Na+ ions have reciprocal effects on agonist versus antagonist interaction with various 7TM receptors. To investigate the Na+ dependence of receptor activation we chose the bradykinin B2 receptor as a prototypic 7TM receptor. Decrease of the intracellular Na+ content from 40 mM to 10 mM of COS-1 cells transiently expressing rat B2 receptors activated the B2 receptor in the absence of agonist as shown by a 3-fold increase in t…

AgonistIntracellular FluidIntrinsic activityReceptor Bradykinin B2medicine.drug_classInositol PhosphatesBradykininIn Vitro TechniquesBradykininLigandsBiochemistryCell Linechemistry.chemical_compoundmedicineAnimalsHumansPoint MutationBradykinin receptorPhosphorylationReceptorG protein-coupled receptorReceptors BradykininSodiumRatschemistryCOS CellsBiophysicsMutagenesis Site-DirectedAlpha-4 beta-2 nicotinic receptorIntracellularBiochemistry
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Conductance and Ion Selectivity of a Mesoscopic Protein Nanopore Probed with Cysteine Scanning Mutagenesis

2005

Nanometer-scale proteinaceous pores are the basis of ion and macromolecular transport in cells and organelles. Recent studies suggest that ion channels and synthetic nanopores may prove useful in biotechnological applications. To better understand the structure-function relationship of nanopores, we are studying the ion-conducting properties of channels formed by wild-type and genetically engineered versions of Staphylococcus aureus alpha-hemolysin (alphaHL) reconstituted into planar lipid bilayer membranes. Specifically, we measured the ion selectivities and current-voltage relationships of channels formed with 24 different alphaHL point cysteine mutants before and after derivatizing the c…

AnionsModels MolecularStaphylococcus aureusCell Membrane PermeabilityBacterial ToxinsLipid BilayersAnalytical chemistryBiophysics02 engineering and technologyIonHemolysin ProteinsStructure-Activity Relationship03 medical and health sciencesCationsNanotechnologyCysteineChannels Receptors and Electrical SignalingLipid bilayerIon channel030304 developmental biologyIons0303 health sciencesChemistrySulfhydryl ReagentsConductance021001 nanoscience & nanotechnologyElectrostaticsElectrophysiologyNanoporeMembraneMutagenesisMutagenesis Site-DirectedBiophysicsGenetic Engineering0210 nano-technologySelectivityBiotechnologyBiophysical Journal
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Secretion and antigenicity of hepatitis B virus small envelope proteins lacking cysteines in the major antigenic region.

1995

Abstract Disulfide bonds are of crucial importance for the structure and antigenic properties of the hepatitis B virus (HBV) envelope. We have evaluated the role of the eight highly conserved cysteines of the major antigenic region for assembly, secretion, and antigenicity of the envelope proteins. Mutants carrying single or multiple substitutions of alanine for cysteine were analyzed using epitope tagging and transient expression in COS-7 cells. The only single cysteines found to be indispensable for efficient secretion were Cys-107 and Cys-138, but double mutation of Cys-137 and Cys-139 also created a block to secretion. Poorly secreted mutants formed aberrant oligomeric structures. The a…

AntigenicityHepatitis B virusGlycosylationmedicine.drug_classMutantMolecular Sequence DataBiologymedicine.disease_causeMonoclonal antibodyEpitopeCell LineViral Envelope ProteinsVirologymedicineAnimalsSecretionCysteineDisulfidesHepatitis B virusAlanineImmunoassayHepatitis B Surface AntigensBase SequenceAntibodies MonoclonalOligonucleotides AntisenseHepatitis BMolecular biologyBiochemistryMutagenesis Site-DirectedCysteineVirology
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The Fumarate/Succinate Antiporter DcuB of Escherichia coli Is a Bifunctional Protein with Sites for Regulation of DcuS-dependent Gene Expression

2008

DcuB of Escherichia coli catalyzes C4-dicarboxylate/succinate antiport during growth by fumarate respiration. The expression of genes of fumarate respiration, including the genes for DcuB (dcuB) and fumarate reductase (frdABCD) is transcriptionally activated by C4-dicarboxylates via the DcuS-DcuR two-component system, comprising the sensor kinase DcuS, which contains a periplasmic sensing domain for C4-dicarboxylates. Deletion or inactivation of dcuB caused constitutive expression of DcuS-regulated genes in the absence of C4-dicarboxylates. The effect was specific for DcuB and not observed after inactivation of the homologous DcuA or the more distantly related DcuC transporter. Random and s…

AntiporterMutantlac operonBiologymedicine.disease_causePeptide MappingBiochemistryAntiportersFumaratesEscherichia colimedicineMolecular BiologyEscherichia coliDerepressionDicarboxylic Acid TransportersIon TransportEscherichia coli ProteinsMutagenesisSuccinatesGene Expression Regulation BacterialCell BiologyPeriplasmic spaceFumarate reductaseDNA-Binding ProteinsSuccinate DehydrogenaseAmino Acid SubstitutionBiochemistryGene Knockdown TechniquesMutagenesis Site-DirectedProtein KinasesTranscription FactorsJournal of Biological Chemistry
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Mutation of the important Tyr-33 residue of chicken avidin: functional and structural consequences

2002

The strong interaction between avidin and biotin is so tight (dissociation constant 10-15M) that conditions usually sufficient for protein denaturing fail to dislodge biotin from the avidin—biotin complex. This kind of irreversible binding hinders the use of avidin in applications such as affinity purification or protein immobilization. To address this concern, we have constructed a series of mutants of the strategically positioned Tyr-33 in order to study the role of this residue in biotin binding, and to create avidin variants with more reversible ligand-binding properties. Unexpectedly, an avidin mutant in which Tyr-33 was replaced with phenylalanine (Avm-Y33F) displayed similar biotin-b…

Biotin bindingBiotinPlasma protein bindingLigandsBiochemistrychemistry.chemical_compoundBiotinAnimalsBinding siteMolecular BiologyBinding SitesMolecular StructurebiologyChemistryTemperatureHydrogen BondingCell BiologyHydrogen-Ion ConcentrationAvidinOxygenDissociation constantBiochemistryBiotinylationMutationMutagenesis Site-Directedbiology.proteinTyrosineProtein quaternary structureEndopeptidase KChickensProtein BindingResearch ArticleAvidinBiochemical Journal
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Regulation of IL-12 p40 Promoter Activity in Primary Human Monocytes: Roles of NF-κB, CCAAT/Enhancer-Binding Protein β, and PU.1 and Identification o…

2001

Abstract Appropriate regulation of IL-12 expression is critical for cell-mediated immune responses. In the present study, we have analyzed the regulation of IL-12 p40 promoter activity in primary human monocytes in vivo. Accordingly, we analyzed the p40 promoter by in vivo footprinting in resting and activated primary human blood CD14+ monocytes. Interestingly, footprints at binding sites for trans-activating proteins such as C/EBP, NF-κB, and ETS were only found upon stimulation with LPS and IFN-γ. In contrast, a footprint over a purine-rich sequence at −155, termed GA-12 (GATA sequence in the IL-12 promoter), was observed in resting, but not activated, cells. Further characterization of t…

CD14ImmunologyDNA FootprintingLipopolysaccharide ReceptorsRepressorBiologyDinoprostoneMonocytesCell LineMicechemistry.chemical_compoundProto-Oncogene ProteinsGene expressionAnimalsHumansImmunology and AllergyBinding sitePromoter Regions GeneticPsychological repressionCells CulturedDNA PrimersBase SequenceCcaat-enhancer-binding proteinsCCAAT-Enhancer-Binding Protein-betaBinding proteinNF-kappa BNuclear ProteinsNF-κBInterleukin-12Molecular biologychemistryMutagenesis Site-DirectedTrans-ActivatorsInterleukin-4The Journal of Immunology
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The Fitness Effects of Random Mutations in Single-Stranded DNA and RNA Bacteriophages

2009

Mutational fitness effects can be measured with relatively high accuracy in viruses due to their small genome size, which facilitates full-length sequencing and genetic manipulation. Previous work has shown that animal and plant RNA viruses are very sensitive to mutation. Here, we characterize mutational fitness effects in single-stranded (ss) DNA and ssRNA bacterial viruses. First, we performed a mutation-accumulation experiment in which we subjected three ssDNA (ΦX174, G4, F1) and three ssRNA phages (Qβ, MS2, and SP) to plaque-to-plaque transfers and chemical mutagenesis. Genome sequencing and growth assays indicated that the average fitness effect of the accumulated mutations was similar…

Cancer Researchlcsh:QH426-470virusesDNA Single-StrandedRNA PhagesBiologymedicine.disease_causeGenomeDNA sequencingGenetics and Genomics/Population GeneticsGeneticsmedicinePoint MutationSelection GeneticMolecular BiologyGenome sizeGenetics (clinical)Ecology Evolution Behavior and SystematicsGeneticsMutationMicrobiology/Microbial Evolution and GenomicsModels GeneticPoint mutationRNARNA PhagesGenetics and Genomics/Microbial Evolution and Genomicslcsh:GeneticsEvolutionary Biology/Microbial Evolution and GenomicsMutagenesisMutationMutagenesis Site-DirectedBacterial virusResearch ArticlePLoS Genetics
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The Process-inducing Activity of Transmembrane Agrin Requires Follistatin-like Domains

2009

Clustering or overexpression of the transmembrane form of the extracellular matrix proteoglycan agrin in neurons results in the formation of numerous highly motile filopodia-like processes extending from axons and dendrites. Here we show that similar processes can be induced by overexpression of transmembrane-agrin in several non-neuronal cell lines. Mapping of the process-inducing activity in neurons and non-neuronal cells demonstrates that the cytoplasmic part of transmembrane agrin is dispensable and that the extracellular region is necessary for process formation. Site-directed mutagenesis reveals an essential role for the loop between beta-sheets 3 and 4 within the Kazal subdomain of t…

Central Nervous SystemFollistatinanimal structuresBiologyCytoplasmic partPC12 CellsBiochemistryProtein Structure SecondaryNeuromuscular junctionCell membraneExtracellular matrixMolecular Basis of Cell and Developmental BiologyProtein structureChlorocebus aethiopsmedicineAnimalsHumansAgrinMolecular BiologyNeuronsAgrinCell MembraneCell BiologyTransmembrane proteinProtein Structure TertiaryRatsCell biologymedicine.anatomical_structurenervous systemProteoglycanBiochemistryCOS CellsMutagenesis Site-Directedbiology.proteinFemaleChickenshormones hormone substitutes and hormone antagonistsJournal of Biological Chemistry
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CtsR is the master regulator of stress response gene expression in Oenococcus oeni.

2005

ABSTRACT Although many stress response genes have been characterized in Oenococcus oeni , little is known about the regulation of stress response in this malolactic bacterium. The expression of eubacterial stress genes is controlled both positively and negatively at the transcriptional level. Overall, negative regulation of heat shock genes appears to be more widespread among gram-positive bacteria. We recently identified an ortholog of the ctsR gene in O. oeni . In Bacillus subtilis , CtsR negatively regulates expression of the clp genes, which belong to the class III family of heat shock genes. The ctsR gene of O. oeni is cotranscribed with the downstream clpC gene. Sequence analysis of t…

ChaperoninsOperonMolecular Sequence DataBiologyMicrobiologyGenome03 medical and health sciencesBacterial ProteinsSigma factorHeat shock proteinOperon[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyGene RegulationPromoter Regions GeneticMolecular BiologyGeneHeat-Shock Proteins030304 developmental biologyRegulator geneOenococcus oeniGeneticsRegulation of gene expressionAdenosine Triphosphatases0303 health sciencesBase Sequence030306 microbiologyCTSRGene Expression Regulation Bacterialbiology.organism_classificationDNA-Binding ProteinsGram-Positive CocciRepressor ProteinsMutagenesis Site-DirectedOenococcus oeniGenome BacterialHeat-Shock ResponseBacillus subtilisMolecular ChaperonesJournal of bacteriology
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