Search results for "Mutant"

showing 10 items of 670 documents

Increased Susceptibility to Skin Carcinogenesis Associated with a Spontaneous Mouse Mutation in the Palmitoyl Transferase Zdhhc13 Gene

2015

International audience; Here we describe a spontaneous mutation in the Zdhhc13 (zinc finger, DHHC domain containing 13) gene (also called Hip14l), one of 24 genes encoding palmitoyl acyltransferase (PAT) enzymes in the mouse. This mutation (Zdhhc13luc) was identified as a nonsense base substitution, which results in a premature stop codon that generates a truncated form of the ZDHHC13 protein, representing a potential loss-of-function allele. Homozygous Zdhhc13luc/Zdhhc13luc mice developed generalized hypotrichosis, associated with abnormal hair cycle, epidermal and sebaceous gland hyperplasia, hyperkeratosis, and increased epidermal thickness. Increased keratinocyte proliferation and accel…

KeratinocytesPathologySkin NeoplasmsMutantMESH: Codon TerminatorMESH: Epidermal Cellsmedicine.disease_causeBiochemistryMESH: Acyltransferases / genetics*MESH: Keratinocytes / physiologyMice0302 clinical medicineHair cycleMESH: AnimalsPalmitoyl acyltransferase0303 health sciencesintegumentary systemNF-kappa B3. Good healthPhenotypemedicine.anatomical_structureNeutrophil Infiltration030220 oncology & carcinogenesisCodon TerminatorKeratinocytemedicine.medical_specialtyClinical SciencesOncology and CarcinogenesisDermatologyBiologyMESH: PhenotypeMESH: Skin Neoplasms / etiologyArticleMESH: Skin Neoplasms / genetics*03 medical and health sciencesMESH: Genetic Predisposition to Disease*medicineAnimalsGenetic Predisposition to DiseaseTerminatorMESH: NF-kappa B / physiologyCodonMESH: MiceMolecular Biology030304 developmental biologyEpidermis (botany)Dermatology & Venereal DiseasesMESH: Leukocyte Elastase / metabolismCell BiologyMESH: Bromodeoxyuridine / metabolismNFKB1Molecular biologyMESH: Neutrophil Infiltration[SDV.GEN.GA]Life Sciences [q-bio]/Genetics/Animal geneticsBromodeoxyuridineEpidermal CellsMutationNIH 3T3 CellsMESH: Mutation*Leukocyte ElastaseCarcinogenesisDHHC domainAcyltransferasesMESH: NIH 3T3 CellsJournal of Investigative Dermatology
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Hydrogen-producingEscherichia colistrains overexpressing lactose permease: FT-IR analysis of the lactose-induced stress

2014

The lactose permease gene (lacY) was overexpressed in the septuple knockout mutant of Escherichia coli, previously engineered for hydrogen production from glucose. It was expected that raising the lactose transporter activity would elevate the intracellular lactose concentration, inactivate the lactose repressor, induce the lactose operon, and as a result stimulate overall lactose consumption and conversion. However, overexpression of the lactose transporter caused a considerable growth delay in the recombinant strain on lactose, resembling to some extent the "lactose killing" phenomenon. Therefore, the recombinant strain was subjected to selection on lactose-containing media. Selection on …

Lactose permeasebiologyProcess Chemistry and TechnologyMutantBiomedical Engineeringlac operonBioengineeringGeneral MedicineLac repressormedicine.disease_causeApplied Microbiology and Biotechnologylaw.inventionchemistry.chemical_compoundBiochemistrychemistrylawDrug DiscoverymedicineRecombinant DNAAlpha-lactalbuminbiology.proteinMolecular MedicineLactoseEscherichia coliBiotechnologyBiotechnology and Applied Biochemistry
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Genetic and Biochemical Analysis of PadR-padC Promoter Interactions during the Phenolic Acid Stress Response in Bacillus subtilis 168

2011

ABSTRACT Bacillus subtilis 168 is resistant to phenolic acids by expression of an inducible enzyme, the phenolic acid decarboxylase (PadC), that decarboxylates these acids into less toxic vinyl derivatives. In the phenolic acid stress response (PASR), the repressor of padC , PadR, is inactivated by these acids. Inactivation of PadR is followed by a strong expression of padC . To elucidate the functional interaction between PadR and the padC promoter, we performed (i) footprinting assays to identify the region protected by PadR, (ii) electrophoretic mobility shift assays (EMSAs) with a modified padC promoter protected region to determine the interacting sequences, and (iii) random mutagenesi…

Leucine zipperMutantRepressorElectrophoretic Mobility Shift AssayGenetics and Molecular BiologyBacillus subtilisBiologyMicrobiologyProtein Structure Secondary03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsStress PhysiologicalBacillus subtilis 168Hydroxybenzoates[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyPromoter Regions GeneticMolecular Biology030304 developmental biology2. Zero hungerchemistry.chemical_classification0303 health sciences030306 microbiologyMutagenesisPhenolic acidGene Expression Regulation Bacterialbiology.organism_classificationMolecular biologyFootprintingEnzymechemistryBiochemistryBacillus subtilisProtein Binding
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Insertion of light-harvesting chlorophyll a/b protein into the thylakoid

2000

The major light-harvesting chlorophyll a/b-binding protein (Lhcb1,2) of photosystem II is inserted into the thylakoid via the signal recognition particle dependent pathway. However, the mechanism by which the protein enters the membrane is at this time unknown. In order to define some topographical restrictions for this process, we constructed several recombinant derivatives of Lhcb1 carrying hexahistidine tags at either protein terminus or in the stromal loop domain. Additionally, green fluorescent protein (GFP) was fused to either terminus. None of the modifications significantly impair the pigment-binding properties of the protein in the in vitro reconstitution of LHCII. With the excepti…

LightPhotosystem IIRecombinant Fusion ProteinsGreen Fluorescent ProteinsPhotosynthetic Reaction Center Complex ProteinsMutantLight-Harvesting Protein ComplexesBiologyThylakoidsBiochemistryInsert (molecular biology)Green fluorescent proteinLight-harvesting complexchemistry.chemical_compoundNickelHistidinePlant ProteinsSignal recognition particlePeasPhotosystem II Protein ComplexBiological TransportIntracellular MembranesPigments BiologicalMolecular WeightLuminescent ProteinschemistryBiochemistryChlorophyllThylakoidMutationBiophysicsCarrier ProteinsEuropean Journal of Biochemistry
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Domain-specific Random Mutagenesis in Light Harvesting Chlorophyll a/b Protein (LHCII)

1998

In all photosynthesising organisms the presence of light harvesting complexes greatly enhances the efficiency of photosynthesis. The most abundant of these pigment binding complexes is the major light harvesting complex II (LHCII) of plants, associated with photosystem II. Its structure has largely been resolved to 3.4 A (1) showing light-harvesting chlorophyll a/b-binding protein (LHCP) with 12 chlorophyll (chl) and 2 xantophyll molecules, all non-covalently arranged around the three membrane spanning domains (MSD) and one amphipathic helix of LHCII. The functional significance of many amino acids in this structure is still unclear, particularly in those parts of the complex that are less …

Light-harvesting complexchemistry.chemical_classificationChlorophyll achemistry.chemical_compoundchemistryPhotosystem IIChlorophyllPigment bindingMutagenesisMutantBiophysicsAmino acid
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Innate immune response triggered by triacyl lipid A is dependent on phospholipid transfer protein (PLTP) gene expression

2010

Hexaacyl lipopolysaccharide (LPS) aggregates in aqueous media, but its partially deacylated lipid A moiety forms monomers with weaker toxicity. Because plasma phospholipid transfer protein (PLTP) transfers hexaacyl LPS, its impact on metabolism and biological activity of triacyl lipid A in mice was addressed. Triacyl lipid A bound readily to plasma high-density lipoproteins (HDLs) when active PLTP was expressed [HDL-associated lipid A after 4.5 h: 59.1+/-16.0% of total in wild-type (WT) vs. 32.5+/-10.3% in PLTP-deficient mice, P0.05]. In the opposite to hexaacyl LPS, plasma residence time of lipid A was extended by PLTP, and proinflammatory cytokines were produced in higher amounts in WT th…

LipopolysaccharideMelanoma ExperimentalBiologyBiochemistryLipid AInterferon-gammaMicechemistry.chemical_compoundCell Line TumorPhospholipid transfer proteinGene expressionGeneticsAnimalsPhospholipid Transfer ProteinsMolecular BiologyCells CulturedChemokine CCL2Interleukin-6Tumor Necrosis Factor-alphaBiological activityMetabolismFlow CytometryMolecular biologyImmunity InnateMice Mutant StrainsInterleukin-10Lipid AGene Expression RegulationchemistryBiochemistryCytokineslipids (amino acids peptides and proteins)Plant lipid transfer proteinsBiotechnologyLipoproteinThe FASEB Journal
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The Host Response toListeria monocytogenesMutants Defective in Genes Encoding Phospholipases C(plcA, plcB)and Actin Assembly(actA)

1997

Several genes involved in the determination of Listeria monocytogenes pathogenesis have been identified. Among them, plcA gene encodes phosphatidylinositol-specific phospholipase C (PI-PLC), plcB gene encodes a broad-range phospholipase C (PC-PLC), and actA encodes a protein contributing to actin assembly in infected cells. The interaction of L. monocytogenes wild type (LO 28) strain and two derivative mutants, plcA- (BUG 206) and actA-/plcB- (LUT 12), with macrophages and T lymphocytes was investigated in a mouse model of listeriosis. Both mutants showed evidence of attenuation. The plcA- mutant, but not the plcB- mutant, expressed an increase in susceptibility to the anti-listerial activi…

LipopolysaccharidesCellular immunityT-LymphocytesImmunologyMutantDose-Response Relationship ImmunologicBiologyLymphocyte ActivationPhosphatidylinositolsmedicine.disease_causeMicrobiologyMicrobiologyMicePhagocytosisListeria monocytogenesVirologyEscherichia colimedicineAnimalsListeriosisGeneEscherichia coliCells CulturedMice Inbred BALB CPhospholipase CWild typeInterleukin-12Listeria monocytogenesActinsGenes BacterialType C PhospholipasesMutationMacrophages PeritonealInterleukin 12FemaleSpleenMicrobiology and Immunology
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Vibrio vulnificus biotype 2 serovar E gne but not galE is essential for lipopolysaccharide biosynthesis and virulence

2008

ABSTRACT This work aimed to establish the role of gne (encoding UDP-GalNAc 4-epimerase activity) and galE (encoding UDP-Gal-4-epimerase activity) in the biosynthesis of surface polysaccharides, as well as in the virulence for eels and humans of the zoonotic serovar of Vibrio vulnificus biotype 2, serovar E. DNA sequence data revealed that gne and galE are quite homologous within this species (≥90% homology). Mutation in gne of strain CECT4999 increased the surface hydrophobicity, produced deep alterations in the outer membrane architecture, and resulted in noticeable increases in the sensitivity to microcidal peptides (MP), to eel and human sera, and to phagocytosis/opsonophagocytosis. Furt…

LipopolysaccharidesLipopolysaccharidePhagocytosisMolecular Sequence DataImmunologyMutantVirulenceVibrio vulnificusMicrobiologyMicrobiologyMiceUDPglucose 4-Epimerasechemistry.chemical_compoundBacterial ProteinsPhagocytosisVibrionaceaeAnimalsCloning MolecularVibrio vulnificusPhagocytesEelsBase SequenceVirulencebiologyChemotaxisTransferrinGene Expression Regulation Bacterialbiology.organism_classificationMolecular PathogenesisComplementationcarbohydrates (lipids)Infectious DiseaseschemistryBiofilmsMutationBacteris patògensParasitologyCarbohydrate EpimerasesBacterial outer membraneAntimicrobial Cationic Peptides
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The lipopolysaccharide O side chain of Vibrio vulnificus serogroup E is a virulence determinant for eels

1997

Vibrio vulnificus is a gram-negative bacterium capable of producing septicemic infections in eels and immunocompromised humans. Two biotypes are classically recognized, with the virulence for eels being specific to strains belonging to biotype 2, which constitutes a homogeneous lipopolysaccharide (LPS)-based O serogroup (which we have designated serogroup E). In the present study we demonstrated that the O side chain of this LPS determines the selective virulence of biotype 2 for eels: (i) biotype 1 strains (which do not belong to serogroup E) are destroyed by the bactericidal action of nonimmune eel serum (NIS) through activation of the alternative pathway of complement, (ii) biotype 2 str…

Lipopolysaccharidesendocrine systemanimal structuresLipopolysaccharideComplement Pathway AlternativeImmunologyMutantVirulenceVibrio vulnificusBiologyMicrobiologyMicrobiologychemistry.chemical_compoundPhagocytosisVibrionaceaeAnimalsVibrioEelsVirulenceO Antigensbiology.organism_classificationVirologyVibrioInfectious DiseaseschemistryAlternative complement pathwayImmunizationParasitologyBacteriaResearch Article
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The role of wild-type and mutated N-ras in the malignant transformation of liver cells

2000

In order to determine the role of N-ras overexpression and mutation in malignant liver cell transformation, wild-type and mutated N-ras were transfected into the rat liver epithelial cell line OC/CDE 22, and N-ras expression, growth kinetics, growth in soft agar, and tumorigenicity in vivo as well as the involvement of the mitogen-activated protein kinase (MAPK) signal transduction pathway in the expression of the malignant phenotype were analyzed. Although OC/CDE 22 cells transfected with wild-type N-ras showed a high expression of N-ras at the mRNA and protein levels, the cells did not grow in soft agar and were not tumorigenic in vivo. In contrast, OC/CDE 22 cells transfected with mutate…

MAPK/ERK pathwayCancer ResearchIn vivoLiver cellMutantWild typeTransfectionSignal transductionBiologyMolecular BiologyMolecular biologyMalignant transformationMolecular Carcinogenesis
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