Search results for "sequence deletion"

showing 10 items of 107 documents

Impaired Transporter Associated with Antigen Processing (TAP) Function Attributable to a Single Amino Acid Alteration in the Peptide TAP Subunit TAP1

2003

Abstract The heterodimeric peptide transporter TAP belongs to the ABC transporter family. Sequence comparisons with the P-glycoprotein and cystic fibrosis transmembrane conductance regulator and the functional properties of selective amino acids in these ABC transporters postulated that the glutamic acid at position 263 and the phenylalanine at position 265 of the TAP1 subunit could affect peptide transporter function. To define the role of both amino acids, TAP1 mutants containing a deletion or a substitution to alanine at position 263 or 265 were generated and stably expressed in murine and human TAP1−/− cells. The different TAP1 mutants were characterized in terms of expression and funct…

Cytotoxicity ImmunologicMacromolecular SubstancesPhenylalanineImmunologyAntigen presentationGlutamic AcidATP-binding cassette transporterEndoplasmic ReticulumTransfectionCell LineMiceAdenosine TriphosphateATP Binding Cassette Transporter Subfamily B Member 3MHC class IAnimalsHumansImmunology and AllergyATP Binding Cassette Transporter Subfamily B Member 2Sequence DeletionAlaninechemistry.chemical_classificationAntigen PresentationbiologyHistocompatibility Antigens Class I3T3 CellsIntracellular MembranesTransporter associated with antigen processingMolecular biologyPeptide FragmentsCystic fibrosis transmembrane conductance regulatorAmino acidMice Inbred C57BLProtein SubunitsAmino Acid SubstitutionBiochemistrychemistryMutagenesis Site-Directedbiology.proteinATP-Binding Cassette TransportersTAP1Sequence AlignmentProtein BindingT-Lymphocytes CytotoxicThe Journal of Immunology
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Nuclear Localization of PTEN by a Ran-dependent Mechanism Enhances Apoptosis: Involvement of an N-Terminal Nuclear Localization Domain and Multiple N…

2006

The targeting of the tumor suppressor PTEN protein to distinct subcellular compartments is a major regulatory mechanism of PTEN function, by controlling its access to substrates and effector proteins. Here, we investigated the molecular basis and functional consequences of PTEN nuclear/cytoplasmic distribution. PTEN accumulated in the nucleus of cells treated with apoptotic stimuli. Nuclear accumulation of PTEN was enhanced by mutations targeting motifs in distinct PTEN domains, and it was dependent on an N-terminal nuclear localization domain. Coexpression of a dominant negative Ran GTPase protein blocked PTEN accumulation in the nucleus, which was also affected by coexpression of importin…

Cèl·lulesAmino Acid MotifsMolecular Sequence DataNuclear Localization SignalsApoptosisBiologyModels BiologicalCatalysislaw.inventionMicelawChlorocebus aethiopsmedicineAnimalsHumansPTENAmino Acid SequenceProteïnes supressores de tumorsMolecular BiologyCells CulturedSequence DeletionCell NucleusCOS cellsEffectorPTEN Phosphohydrolase3T3 CellsArticlesCell BiologyProtein Structure TertiaryRatsTransport proteinProtein TransportCell nucleusran GTP-Binding Proteinmedicine.anatomical_structureCOS CellsRanbiology.proteinCancer researchSuppressorNuclear localization sequenceHeLa CellsMolecular Biology of the Cell
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Conjugative plasmid pIP501 undergoes specific deletions after transfer from Lactococcus lactis to Oenococcus oeni

2003

Conjugal transfer of plasmids pIP501 and its derivative pVA797 from Lactococcus lactis to Oenococcus oeni was assayed by filter mating. Plasmid pIP501 was transferred to a number of O. oeni strains whereas a single transconjugant of O. oeni M42 was recovered when pVA797 was used. Physical analysis of the transconjugant plasmids revealed that pIP501 and pVA797 underwent extensive deletions in O. oeni that affected the tra region (conjugal transfer) and SegB region (stability). All derivatives showed segregational instability in O. oeni, but were stably maintained in L. lactis. These differences correlated with the different plasmid copy numbers and the extent of deletions within the SegB reg…

DNA BacterialMolecular Sequence DataRestriction Mappingmedicine.disease_causeBiochemistryMicrobiologyPlasmidGene OrderGeneticsmedicineAmino Acid SequenceMolecular BiologySequence DeletionOenococcus oeniGeneticsMutationBase SequencebiologyStrain (chemistry)Lactococcus lactisConjugative plasmidGeneral Medicinebiology.organism_classificationStreptococcaceaeGram-Positive CocciLactococcus lactisGenes BacterialConjugation GeneticGene DeletionLeuconostocBacteriaPlasmidsArchives of Microbiology
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The Rate and Molecular Spectrum of Spontaneous Mutations in Arabidopsis thaliana

2010

Evolution in Action Rates of evolution in gene and genome sequences have been estimated, but these estimates are subject to error because many of the steps of evolution over the ages are not directly measurable or are hidden under subsequent changes. Ossowski et al. (p. 92 ) now provide a more accurate measurement of how often spontaneous mutations arise in a nuclear genome. Mutations arising over 30 generations were compared by sequencing DNA from individual Arabidopsis thaliana plants. UV- and deamination-induced mutagenesis appeared to bias the type of mutations found.

DNA PlantUltraviolet RaysMutantArabidopsismedicine.disease_causeArticlechemistry.chemical_compoundCytosineINDEL MutationArabidopsismedicineArabidopsis thalianaSequence DeletionGeneticsMutationMultidisciplinarybiologyMutagenesisSequence Analysis DNAMutation AccumulationDNA Methylationbiology.organism_classificationMolecular biologychemistryDeaminationMutationDNA IntergenicINDEL MutationCytosineGenome Plant
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Impact of a Three Amino Acid Deletion in the CH2 Domain of Murine IgG1 on Fc-Associated Effector Functions

2008

Abstract Four murine IgG subclasses display markedly different Fc-associated effector functions because of their differential binding to three activating IgG Fc receptors (FcγRI, FcγRIII, and FcγRIV) and C1q. Previous analysis of IgG subclass switch variants of 34-3C anti-RBC monoclonal autoantibodies revealed that the IgG1 subclass, which binds only to FcγRIII and fails to activate complement, displayed the poorest pathogenic potential. This could be related to the presence of a three amino acid deletion at positions 233–235 in the CH2 domain uniquely found in this subclass. To address this question, IgG1 insertion and IgG2b deletion mutants at positions 233–235 of 34-3C anti-RBC Abs were …

Deletion mutantImmunologyAntibody AffinityDown-Regulationddc:616.07BiologySubclassProtein Structure Tertiary/geneticsMiceAnimalsImmunology and AllergyAmino AcidsEffector functionsSequence DeletionMice Knockoutchemistry.chemical_classificationMice Inbred BALB CMice Inbred NZBAnemia Hemolytic Autoimmune/genetics/immunologyReceptors IgGAutoantibodyAmino Acids/chemistry/genetics/metabolismIgg subclassesReceptors IgG/antagonists & inhibitors/genetics/metabolismPathogenicityProtein Structure TertiaryImmunoglobulin G/genetics/metabolismImmunoglobulin Switch RegionCell biologyAmino acidImmunoglobulin Heavy Chains/biosynthesis/genetics/metabolismAntibody Affinity/geneticsBiochemistrychemistryImmunoglobulin GMonoclonalMutagenesis Site-DirectedAnemia Hemolytic AutoimmuneDown-Regulation/genetics/immunologyImmunoglobulin Heavy ChainsThe Journal of Immunology
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Neuronal precursor-specific activity of a human doublecortin regulatory sequence.

2005

The doublecortin (DCX) gene encodes a 40-kDa microtubule-associated protein specifically expressed in neuronal precursors of the developing and adult CNS. Due to its specific expression pattern, attention was drawn to DCX as a marker for neuronal precursors and neurogenesis, thereby underscoring the importance of its promoter identification and promoter analysis. Here, we analysed the human DCX regulatory sequence and confined it to a 3.5-kb fragment upstream of the ATG start codon. We demonstrate by transient transfection experiments that this fragment is sufficient and specific to drive expression of reporter genes in embryonic and adult neuronal precursors. The activity of this regulator…

Doublecortin Domain ProteinsDoublecortin Protein5' Flanking RegionBlotting WesternMolecular Sequence DataRegulatory Sequences Nucleic AcidTransfectionBiochemistryHippocampusCellular and Molecular NeuroscienceMiceGene expressionAnimalsHumansCell LineageGrowth SubstancesGeneTranscription factorCells CulturedSequence DeletionRegulation of gene expressionNeuronsReporter genebiologyBase SequenceStem CellsNeurogenesisNeuropeptidesBrainSequence Analysis DNAMolecular biologyDoublecortinMice Inbred C57BLGene Expression RegulationRegulatory sequencebiology.proteinMicrotubule-Associated ProteinsJournal of neurochemistry
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Binding of Escherichia coli hemolysin and activation of the target cells is not receptor-dependent.

2005

Abstract Production of a single cysteine substitution mutant, S177C, allowed Escherichia coli hemolysin (HlyA) to be radioactively labeled with tritiated N-ethylmaleimide without affecting biological activity. It thus became possible to study the binding characteristics of HlyA as well as of toxin mutants in which one or both acylation sites were deleted. All toxins bound to erythrocytes and granulocytes in a nonsaturable manner. Only wild-type toxin and the lytic monoacylated mutant stimulated production of superoxide anions in granulocytes. An oxidative burst coincided with elevation of intracellular Ca2+, which was likely because of passive influx of Ca2+ through the toxin pores. Competi…

ErythrocytesAcylationMutantBacterial ToxinsBiologymedicine.disease_causeBiochemistryHemolysin ProteinsSuperoxidesmedicineEscherichia coliHumansReceptorMolecular BiologyEscherichia coliRespiratory BurstSequence DeletionBinding SitesToxinHemolysinBiological activityCell BiologyMolecular biologyLymphocyte Function-Associated Antigen-1Respiratory burstBiochemistryAmino Acid SubstitutionMutationMutagenesis Site-DirectedbacteriaCalciumK562 CellsIntracellularGranulocytesThe Journal of biological chemistry
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Expression of Active Streptolysin O in Escherichia coli as a Maltose-Binding-Protein-Streptolysin-O Fusion Protein. The N-Terminal 70 Amino Acids are…

1996

Streptolysin 0 (SLO) is the prototype of a family of cytolysins that consists of proteins which bind to cholesterol and form very large transmembrane pores. Structure/function studies on the pore-forming cytolysin SLO have been complicated by the proteolytic inactivation of a substantial portion of recombinant SLO (rSLO) expressed in Escherichia coli. To overcome this problem, translational fusions between the E. coli maltose-binding protein (MBP) gene and SLO were constructed, using the vectors pMAL-p2 and pMAL-c2. MBP-SLO fusion proteins were degraded if secreted into the E. coli periplasm, but intact, soluble MBP-SLO fusion proteins were produced at high levels in the cytoplasm. Active S…

ErythrocytesMonosaccharide Transport Proteinsgenetic structuresProtein ConformationStreptococcus pyogenesRecombinant Fusion ProteinsMolecular Sequence Datamedicine.disease_causeHemolysisBiochemistryMaltose-Binding ProteinsStructure-Activity RelationshipMaltose-binding proteinProtein structureBacterial ProteinsEscherichia colimedicineHumansCloning MolecularEscherichia coliSequence DeletionPore-forming toxinBase SequencebiologyEscherichia coli ProteinsFluoresceinsFusion proteineye diseasesTransmembrane proteinBiochemistryLiposomesStreptolysinsbiology.proteinATP-Binding Cassette TransportersStreptolysinsense organsCytolysinCarrier ProteinsSequence AnalysisEuropean Journal of Biochemistry
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Expression of the Anti-amyloidogenic Secretase ADAM10 Is Suppressed by Its 5′-Untranslated Region*

2010

Proteolytic processing of the amyloid precursor protein by alpha-secretase prevents formation of the amyloid beta-peptide (Abeta), which is the main constituent of amyloid plaques in brains of Alzheimer disease (AD) patients. alpha-Secretase activity is decreased in AD, and overexpression of the alpha-secretase ADAM10 (a disintegrin and metalloprotease 10) in an AD animal model prevents amyloid pathology. ADAM10 has a 444-nucleotide-long, very GC-rich 5'-untranslated region (5'-UTR) with two upstream open reading frames. Because similar properties of 5'-UTRs are found in transcripts of many genes, which are regulated by translational control mechanisms, we asked whether ADAM10 expression is…

Five prime untranslated regionenzymology [Brain]ADAM10ADAM10 protein humanBACE1-ASgenetics [Amyloid Precursor Protein Secretases]genetics [Alzheimer Disease]genetics [ADAM Proteins]BiochemistryGene Expression Regulation Enzymologicbiosynthesis [Membrane Proteins]ADAM10 ProteinAlzheimer DiseaseChlorocebus aethiopsAmyloid precursor proteinProtein biosynthesisbiosynthesis [Amyloid beta-Peptides]genetics [Amyloid beta-Peptides]AnimalsHumansGene RegulationMolecular BiologySequence Deletionbiosynthesis [ADAM Proteins]Amyloid beta-PeptidesbiologyBase SequenceP3 peptideenzymology [Alzheimer Disease]BrainMembrane ProteinsCell BiologyMolecular biologyBiochemistry of Alzheimer's diseasegenetics [Membrane Proteins]ADAM Proteinsbiosynthesis [Amyloid Precursor Protein Secretases]Protein Biosynthesisddc:540COS Cellsbiology.proteinAmyloid Precursor Protein Secretases5' Untranslated RegionsAmyloid precursor protein secretase
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Homozygous deletion of ATC1 and NTC1 genes in Candida parapsilosis abolishes trehalase activity and affects cell growth, sugar metabolism, stress res…

2015

A double homozygous atc1Δ/atc1Δ/ntc1Δ/ntc1Δ mutant (atc1Δ/ntc1Δ KO) was constructed in the pathogen opportunistic yeast Candida parapsilosis by disruption of the two chromosomal alleles coding for NTC1 gene (encoding a neutral trehalase) in a Cpatc1Δ/atc1Δ background (atc1Δ KO strain, deficient in acid trehalase). The Cpatc1Δ/ntc1Δ KO mutant failed to counteract the inability of Cpatc1Δ cells to metabolize exogenous trehalose and showed a similar growth pattern on several monosaccharides and disaccharides. However, upon prolonged incubation in either rich medium (YPD) or nutrient-starved medium the viability of Cpatc1Δ cells exhibited a sensitive phenotype, which was augmented by further Cp…

Fungal proteinVirulencebiologyMutantTrehalase activityTrehaloseCandida parapsilosisbiology.organism_classificationMicrobiologyTrehaloseYeastMicrobiologyFungal ProteinsOxidative Stresschemistry.chemical_compoundchemistryStress PhysiologicalBiofilmsGeneticsCarbohydrate MetabolismTrehalaseTrehalaseGene knockoutCandidaSequence DeletionFungal Genetics and Biology
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