Search results for "genetic complementation"

showing 10 items of 35 documents

Gene amplification in fibroblasts from ataxia telangiectasia (AT) patients and in X-ray hypersensitive AT-like Chinese hamster mutants.

2001

In search of functions involved in the regulation of gene amplification, and given the relevance of chromosome breakage in initiating the process, we analyzed the gene amplification ability of cells hypersensitive to inducers of DNA double-strand breaks and defective in cell cycle control: two human fibroblast strains derived from patients affected by ataxia telangiectasia (AT) and two hamster mutant cell lines belonging to complementation group XRCC8 of the rodent X-ray-sensitive mutants. These mutants are considered hamster models of AT cells. To measure gene amplification, the frequency and the rate of occurrence of N-(phosphonacetyl)-L-aspartate resistant cells were determined. In both …

Phosphonoacetic AcidCancer ResearchAntimetabolites AntineoplasticMutantHamstermedicine.disease_causeRadiation ToleranceChinese hamsterCell LineAtaxia TelangiectasiaCricetulusMultienzyme ComplexesCricetinaeGene duplicationmedicineAspartate CarbamoyltransferaseAnimalsHumansDihydroorotaseMutationAspartic AcidbiologyX-RaysGenetic Complementation TestGene AmplificationGeneral MedicineCell cycleFibroblastsmedicine.diseasebiology.organism_classificationMolecular biologyDrug Resistance NeoplasmAtaxia-telangiectasiaMutationCarbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)Chromosome breakageCarcinogenesis
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Thermostability of Two Cyanobacterial GrpE Thermosensors

2011

GrpE proteins act as co-chaperones for DnaK heat-shock proteins. The dimeric protein unfolds under heat stress conditions, which results in impaired interaction with a DnaK protein. Since interaction of GrpE with DnaK is crucial for the DnaK chaperone activity, GrpE proteins act as a thermosensor in bacteria. Here we have analyzed the thermostability and function of two GrpE homologs of the mesophilic cyanobacterium Synechocystis sp. PCC 6803 and of the thermophilic cyanobacterium Thermosynechococcus elongatus BP1. While in Synechocystis an N-terminal helix pair of the GrpE dimer appears to be the thermosensing domain and mainly mediates GrpE dimerization, the C-terminal four-helix bundle i…

PhysiologyMolecular Sequence DataProtein domainPlant SciencePlasma protein bindingCyanobacteriaProtein structureBacterial ProteinsHeat shock proteinEscherichia coliAmino Acid SequencePeptide sequenceHeat-Shock ProteinsThermostabilitySequence Homology Amino AcidbiologyProtein StabilityChemistryCircular DichroismGenetic Complementation TestSynechocystisSynechocystisTemperatureCell BiologyGeneral Medicinebiology.organism_classificationProtein Structure TertiaryCross-Linking ReagentsChaperone (protein)Biophysicsbiology.proteinbacteriaProtein MultimerizationProtein BindingPlant and Cell Physiology
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The Arabidopsis COPT6 Transport Protein Functions in Copper Distribution Under Copper-Deficient Conditions

2013

Copper (Cu), an essential redox active cofactor, participates in fundamental biological processes, but it becomes highly cytotoxic when present in excess. Therefore, living organisms have established suitable mechanisms to balance cellular and systemic Cu levels. An important strategy to maintain Cu homeostasis consists of regulating uptake and mobilization via the conserved family of CTR/COPT Cu transport proteins. In the model plant Arabidopsis thaliana, COPT1 protein mediates root Cu acquisition, whereas COPT5 protein functions in Cu mobilization from intracellular storage organelles. The function of these transporters becomes critical when environmental Cu bioavailability diminishes. Ho…

PhysiologyMolecular Sequence DataSaccharomyces cerevisiaeMutantArabidopsisSaccharomyces cerevisiaePlant SciencePlant RootsCofactorCell membraneGene Expression Regulation PlantArabidopsisOrganellemedicineHomeostasisAmino Acid SequenceSLC31 ProteinsbiologyArabidopsis ProteinsMembrane transport proteinCell MembraneGenetic Complementation TestMembrane Transport ProteinsBiological TransportCell BiologyGeneral MedicinePlants Genetically Modifiedbiology.organism_classificationUp-RegulationTransport proteinCell biologyPlant LeavesMutagenesis Insertionalmedicine.anatomical_structureBiochemistrySeedsbiology.proteinPlant Vascular BundleSequence AlignmentCopperPlant ShootsPlant and Cell Physiology
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Functional characterization of the plastidial 3-phosphoglycerate dehydrogenase family in Arabidopsis.

2013

This work contributes to unraveling the role of the phosphorylated pathway of serine (Ser) biosynthesis in Arabidopsis (Arabidopsis thaliana) by functionally characterizing genes coding for the first enzyme of this pathway, 3-phosphoglycerate dehydrogenase (PGDH). We identified two Arabidopsis plastid-localized PGDH genes (3-PGDH and EMBRYO SAC DEVELOPMENT ARREST9 [EDA9]) with a high percentage of amino acid identity with a previously identified PGDH. All three genes displayed a different expression pattern indicating that they are not functionally redundant. pgdh and 3-pgdh mutants presented no drastic visual phenotypes, but eda9 displayed delayed embryo development, leading to aborted emb…

PhysiologyMutantMolecular Sequence DataArabidopsisPlant SciencePlant RootsGene Expression Regulation EnzymologicSerineBiochemistry and MetabolismGene Expression Regulation PlantComplementary DNAArabidopsisGeneticsSerineArabidopsis thalianaMetabolomicsAmino Acid SequencePlastidsPhosphorylationGenePhosphoglycerate DehydrogenasePhylogenyTapetumMicroscopy ConfocalbiologySequence Homology Amino AcidArabidopsis ProteinsReverse Transcriptase Polymerase Chain ReactionGenetic Complementation Testfood and beveragesPlant Components Aerialbiology.organism_classificationPlants Genetically ModifiedPhenotypeIsoenzymesBiochemistryMultigene FamilyMutationSeedsPollenPlant physiology
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A critical role of plastidial glycolytic Glyceraldehyde-3-Phosphate Dehydrogenase in the control of plant metabolism and development

2009

3 páginas.

PlastidArabidopsisDehydrogenasePlant ScienceSerine biosynthesisGenes PlantPlant RootsGene Expression Regulation EnzymologicSerinechemistry.chemical_compoundBiosynthesisGene Expression Regulation PlantSerineGlycolysisRNA MessengerPlastidsAmino AcidsPhosphorylationPhylogenyGlyceraldehyde 3-phosphate dehydrogenasebiologyArabidopsis ProteinsGAPDHGenetic Complementation TestGlyceraldehyde-3-Phosphate DehydrogenasesMetabolismLipid MetabolismArticle AddendumPlant LeavesProtein TransportCytosolMetabolic pathwayPhenotypeBiochemistrychemistryMutationbiology.proteinCarbohydrate MetabolismGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)GlycolysisResearch Article
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Diverse cell surface protein ectodomains are shed by a system sensitive to metalloprotease inhibitors.

1996

The extracellular domains of a diverse group of membrane proteins are shed in response to protein kinase C activators such as phorbol 12-myristate 13-acetate (PMA). The lack of sequence similarity in the cleavage sites suggests the involvement of many proteases of diverse specificity in this process. However, a mutant Chinese hamster ovary cell line recently isolated for being defective in PMA-activated shedding of the membrane-anchored growth factor transforming growth factor alpha precursor (proTGF-alpha) is concomitantly defective in the shedding of many other unrelated membrane proteins. Here we show that independent mutagenesis and selection experiments yield shedding mutants having th…

ProteasesCellCHO CellsBiologyHydroxamic AcidsTransfectionBiochemistryAmyloid beta-Protein PrecursorAntigens CDCricetinaemedicineAnimalsProtease InhibitorsL-SelectinProtein PrecursorsCell adhesionMolecular BiologyProtein kinase CMetalloproteinaseChinese hamster ovary cellCell MembraneGenetic Complementation TestMembrane ProteinsMetalloendopeptidasesCell BiologyReceptors InterleukinTransforming Growth Factor alphaReceptors Interleukin-6Cell biologyKineticsmedicine.anatomical_structurePhenotypeEctodomainMembrane proteinMutagenesisTetradecanoylphorbol AcetatePhenanthrolinesThe Journal of biological chemistry
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Complementation of Saccharomyces cerevisiae mutationsin genes involved in translation and protein folding (EFB1 and SSB1)with Candida albicans cloned…

2000

We have demonstrated that the expression of Candida albicans genes involved in translation and protein folding (EFB1 and SSB1) complements the phenotype of Saccharomyces cerevisiae mutants. The elongation factor 1beta (EF-1beta) is essential for growth and efb1 S. cerevisiae null mutant cells are not viable; however, viable haploid cells, carrying the disrupted chromosomal allele of the S. cerevisiae EFB1 gene and pEFB1, were isolated upon sporulation of a diploid strain which was heterozygous at the EFB1 locus and transformed with pEFB1 (a pEMBLYe23 derivative plasmid containing an 8-kb DNA fragment from the C. albicans genome which contains the EFB1 gene). This indicates that the C. albic…

Protein FoldingSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeMutantSaccharomyces cerevisiaeMicrobiologyPeptide Elongation Factor 1Transformation GeneticGene Expression Regulation FungalHeat shock proteinCandida albicansProtein biosynthesisHSP70 Heat-Shock ProteinsCandida albicansMolecular BiologyGenebiologyGenetic Complementation TestTemperatureGeneral Medicinebiology.organism_classificationMolecular biologyComplementationProtein BiosynthesisChaperone (protein)Mutationbiology.proteinResearch in Microbiology
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Molecular cloning of the RPS0 gene from Candida tropicalis.

2001

The Saccharomyces cerevisiae RPS0 A and B genes encode proteins essential for maturation of the 40S ribosomal subunit precursors. We have isolated a homologue of the RPS0 gene from Candida tropicalis, which we named CtRPS0. The C. tropicalisRPS0 encodes a protein of 261 amino acid residues with a predicted molecular weight of 28.65 kDa and an isoelectric point of 4.79. CtRps0p displays significant amino acid sequence homology with Rps0p from C. albicans, S. cerevisiae, Neurospora crassa, Schizosaccharomyces pombe, Pneumocystis carinii and higher organisms, such as human, mouse and rat. CtRPS0 on a high copy number vector can complement the lethal phenotype linked to the disruption of both R…

Ribosomal ProteinsSaccharomyces cerevisiaeGenes FungalMolecular Sequence DataBioengineeringSaccharomyces cerevisiaeBiologyApplied Microbiology and BiotechnologyBiochemistryNeurospora crassaCandida tropicalisFungal ProteinsRibosomal proteinGeneticsAmino Acid SequenceCloning MolecularGeneSouthern blotCandidaGeneticsBase SequenceSequence Homology Amino AcidGenetic Complementation TestNucleic acid sequencebiology.organism_classificationSchizosaccharomyces pombeProtein Processing Post-TranslationalBiotechnologyYeast (Chichester, England)
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The Histidinol Phosphate Phosphatase Involved in Histidine Biosynthetic Pathway Is Encoded by SCO5208 (hisN) in Streptomyces coelicolor A3(2)

2008

Through the screening of a Streptomyces coelicolor genomic library, carried out in a histidinol phosphate phosphatase (HolPase) deficient strain, SCO5208 was identified as the last unknown gene involved in histidine biosynthesis. SCO5208 is a phosphatase, and it can restore the growth in minimal medium in this HolPase deficient strain when cloned in a high or low copy number vector. Moreover, it shares sequence homology with other HolPases recently identified in Actinobacteria. During this work a second phosphatase, SCO2771, sharing no homologies with SCO5208 and all so far described phosphatases was identified. It can complement HolPase activity mutation only at high copy number. Sequence …

Sequence analysisPhosphataseDNA Mutational AnalysisMolecular Sequence DataMutation MissenseStreptomyces coelicolormedicine.disease_causeApplied Microbiology and BiotechnologyMicrobiologyBacterial ProteinsHistidinol Phosphate Phosphatase Histidine Biosynthesis Streptomyces coelicolormedicineGenomic libraryHistidineAmino Acid SequenceGeneHistidineGeneticsMutationbiologySequence Homology Amino AcidStreptomyces coelicolorGenetic Complementation TestHistidinol-PhosphataseGeneral Medicinebiology.organism_classificationBiosynthetic PathwaysBiochemistryMutant ProteinsLow copy number
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Host-Nonspecific Iron Acquisition Systems and Virulence in the Zoonotic Serovar of Vibrio vulnificus

2014

ABSTRACT The zoonotic serovar of Vibrio vulnificus (known as biotype 2 serovar E) is the etiological agent of human and fish vibriosis. The aim of the present work was to discover the role of the vulnibactin- and hemin-dependent iron acquisition systems in the pathogenicity of this zoonotic serovar under the hypothesis that both are host-nonspecific virulence factors. To this end, we selected three genes for three outer membrane receptors ( vuuA , a receptor for ferric vulnibactin, and hupA and hutR , two hemin receptors), obtained single and multiple mutants as well as complemented strains, and tested them in a series of in vitro and in vivo assays, using eels and mice as animal models. Th…

SerotypeVirulence FactorsSequence analysisIronImmunologyVirulenceVibrio vulnificusBiologyMicrobiologyMicrobiologyGene Knockout TechniquesMiceVibrio InfectionsAnimalsNatural reservoirOxazolesVibrio vulnificusGeneMice Inbred BALB CVirulenceGenetic Complementation TestMembrane Transport ProteinsBacterial Infectionsbiology.organism_classificationAmidesDisease Models AnimalInfectious DiseasesVibrio InfectionsHeminParasitologyBacterial outer membraneInfection and Immunity
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