Search results for "mutant"

showing 10 items of 670 documents

Glycoprotein molecules in the walls of Schizosaccharomyces pombe wild-type cells and a morphologically altered mutant resistant to papulacandin B

1990

SUMMARY: Schizosaccharomyces pombe cell walls contain two major glycoprotein species, I and II, with molecular masses of 2 x 106 and 5 x 105 Da respectively, as determined by gel filtration chromatography and PAGE. The ratio of sugar to protein is higher in species I than in species II. Much of the sugar in both glycoproteins (about 85% in wild-type cells) is O-linked to the peptide moiety. The morphological sph1 mutant is resistant to papulacandin B, and its cell wall contains less glycoprotein II (but not less glycoprotein I) than the parental wild-type strain, although glycoprotein II is still synthesized and released into the growth medium. Papulacandin B largely reverses the morphologi…

Antifungal AgentsHydrolasesMutantCarbohydratesDrug ResistancePapulacandin BBiologyCell morphologyMicrobiologyCell wallchemistry.chemical_compoundCell WallAcetylglucosaminidaseSchizosaccharomycesGlycoproteinsGel electrophoresischemistry.chemical_classificationWild typebiology.organism_classificationAnti-Bacterial AgentsCulture MediaMolecular WeightAminoglycosidesMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseSolubilityBiochemistrychemistryMutationSchizosaccharomyces pombeChromatography GelGlycoproteinJournal of General Microbiology
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Isolation and characterization of Saccharomyces cerevisiae mutants resistant to aculeacin A

1991

Aculeacin A is a lipopeptide that inhibits beta-glucan synthesis in yeasts. A number of Saccharomyces cerevisiae mutants resistant to this antibiotic were isolated, and four loci (ACR1, ACR2, ACR3, and ACR4) whose products are involved in the sensitivity to aculeacin A of yeast cells were defined. Mutants containing mutations in the four loci were also resistant to echinocandin B, another member of this lipopeptide family of antibiotics. In contrast, acr1, acr3, and acr4 mutants were resistant to papulacandin B (an antibiotic containing a disaccharide linked to two fatty acid chains that also inhibits beta-glucan synthesis), but acr2 mutants were susceptible to this antibiotic. This result …

Antifungal AgentsLlevat de cervesaGenotypeMutantSaccharomyces cerevisiaePapulacandin BSaccharomyces cerevisiaemedicine.disease_causePeptides CyclicMicrobiologyFungal ProteinsEchinocandinschemistry.chemical_compoundCell WallEchinocandin BmedicinePharmacology (medical)PharmacologyFungal proteinMutationbiologyMutagenicity TestsMembrane ProteinsLipopeptideAminoglicòsidbiology.organism_classificationYeastAnti-Bacterial AgentsAminoglucòsidsAminoglycosidesInfectious DiseaseschemistryBiochemistryGlucosyltransferasesMutationSchizosaccharomyces pombe ProteinsPeptidesResearch Article
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Dosage-dependent roles of the Cwt1 transcription factor for cell wall architecture, morphogenesis, drug sensitivity and virulence in Candida albicans.

2009

The Cwt1 transcription factor is involved in cell wall architecture of the human fungal pathogen Candida albicans. We demonstrate here that deficiency of Cwt1 leads to decreased β1,6-glucan in the cell wall, while mannoproteins are increased in the cell wall of exponentially growing cells and are released into the medium of stationary phase cells. Hyphal morphogenesis of cwt1 mutants is reduced on the surfaces of some inducing media. Unexpectedly, the CWT1/cwt1 heterozygous strains shows some stronger in vitro phenotypes compared to the homozygous mutant. The heterozygous but not the homozygous strain is also strongly impaired for its virulence in a mouse model of systemic infection. We sug…

Antifungal AgentsMutantMorphogenesisGene DosageHyphaeVirulenceBioengineeringApplied Microbiology and BiotechnologyBiochemistryMicrobiologyCell wallFungal ProteinsMiceCell WallDrug Resistance FungalGene Expression Regulation FungalCandida albicansGeneticsMorphogenesisAnimalsHumansCandida albicansDNA FungalTranscription factorOligonucleotide Array Sequence AnalysisMembrane GlycoproteinsbiologyVirulenceHomozygoteCandidiasisbiology.organism_classificationPhenotypeCorpus albicansMutationBiotechnologyTranscription FactorsYeast (Chichester, England)
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A role for the MAP kinase gene MKC1 in cell wall construction and morphological transitions in Candida albicans.

1998

The Candida albicans MKC1 gene encodes a mitogen-activated protein (MAP) kinase, which has been cloned by complementation of the lytic phenotype associated with Saccharomyces cerevisiae slt2 (mpk1) mutants. In this work, the physiological role of this MAP kinase in the pathogenic fungus C. albicans was characterized and a role for MKC1 in the biogenesis of the cell wall suggested based on the following criteria. First, C. albicans mkc1Δ/mkc1Δ strains displayed alterations in their cell surfaces under specific conditions as evidenced by scanning electron microscopy. Second, an increase in specific cell wall epitopes (O-glycosylated mannoprotein) was shown by confocal microscopy in mkc1Δ/mkc1…

Antifungal AgentsTranscription GeneticSaccharomyces cerevisiaeMutantMAP Kinase Kinase 2MAP Kinase Kinase 1ChitinSaccharomyces cerevisiaeProtein Serine-Threonine KinasesMicrobiologyGene Expression Regulation EnzymologicFungal ProteinsPseudohyphal growthCell WallGene Expression Regulation FungalCandida albicansCandida albicansDNA FungalFluorescent Antibody Technique IndirectGlucansProtein Kinase CMitogen-Activated Protein Kinase KinasesRecombination GeneticMembrane GlycoproteinsMicroscopy ConfocalbiologyKinaseProtein-Tyrosine Kinasesbiology.organism_classificationFlow Cytometrybeta-GalactosidaseCorpus albicansComplementationMicroscopy ElectronBiochemistryMitogen-activated protein kinaseCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMicroscopy Electron ScanningMitogen-Activated Protein KinasesPlasmidsMicrobiology (Reading, England)
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Role of the Non-Canonical RNAi Pathway in the Antifungal Resistance and Virulence of Mucorales

2021

Mucorales are the causal agents for the lethal disease known as mucormycosis. Mortality rates of mucormycosis can reach up to 90%, due to the mucoralean antifungal drug resistance and the lack of effective therapies. A concerning urgency among the medical and scientific community claims to find targets for the development of new treatments. Here, we reviewed different studies describing the role and machinery of a novel non-canonical RNAi pathway (NCRIP) only conserved in Mucorales. Its non-canonical features are the independence of Dicer and Argonaute proteins. Conversely, NCRIP relies on RNA-dependent RNA Polymerases (RdRP) and an atypical ribonuclease III (RNase III). NCRIP regulates the…

AntifungalTransposable element0301 basic medicineMucoralesAntifungal Agentstransposonmedicine.drug_classRNA Stability030106 microbiologyAntifungal drugVirulenceReviewQH426-470mucormycosis03 medical and health sciencesDrug Resistance FungalRNA interferenceFongsmedicineGeneticsbiochemistryRNA MessengerRibonuclease IIIepimutantGenetics (clinical)Genome stabilityGeneticsRdRPR3B2biologyMucormycosisnon-canonical RNAiRNA FungalArgonauteantifungal resistancemedicine.diseasebiology.organism_classificationvirulenceRNA silencing030104 developmental biologyNon canonicalbiology.proteinInfeccióMucoralesRNA Interferencegenome stabilitySignal TransductionDicerGenes
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Neutrophil extracellular traps arm DC vaccination against NPM-mutant myeloproliferation

2021

AbstractNeutrophil extracellular traps (NET) are web-like chromatin structures composed by dsDNA and histones, decorated with anti-microbial proteins. Their interaction with dendritic cells (DC) allows DC activation and maturation toward presentation of NET-associated antigens. Differently from other types of cell death that imply protein denaturation, NETosis preserves the proteins localized onto the DNA threads for proper enzymatic activity and conformational status, including immunogenic epitopes. Besides neutrophils, leukemic cells can release extracellular traps displaying leukemia-associated antigens, prototypically mutant nucleophosmin (NPMc+) that upon mutation translocates from nuc…

AntigenChemistryCytoplasmMutantMyeloproliferationCytotoxic T cellNeutrophil extracellular trapsCD8EpitopeCell biology
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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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Proteomic Analysis of Saccharomyces cerevisiae Response to Oxidative Stress Mediated by Cocoa Polyphenols Extract

2020

The present study addressed the protective effects against oxidative stress (OS) of a cocoa powder extract (CPEX) on the protein expression profile of S. cerevisiae. A proteomic analysis was performed after culture preincubation with CPEX either without stress (&minus

Antioxidantmedicine.medical_treatmentSaccharomyces cerevisiaePharmaceutical Scienceantioxidant activitySaccharomyces cerevisiaeamino acid metabolismmedicine.disease_causeAmino acid metabolismAnalytical Chemistrycocoa polyphenolslcsh:QD241-441<i>Saccharomyces cerevisiae</i>03 medical and health sciencesHistone H3chemistry.chemical_compoundBiosynthesisAntioxidant activitylcsh:Organic chemistryprotein identificationDrug DiscoverymedicineDeletion mutantsoxidative stressPhysical and Theoretical ChemistryReactive oxygen species metabolic process030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyCocoa polyphenolsChemistry030302 biochemistry & molecular biologyOrganic Chemistrybiology.organism_classificationYeastAmino acidBiochemistryChemistry (miscellaneous)Oxidative stressMolecular MedicineProtein identificationdeletion mutantsOxidative stressMolecules
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DctA- and Dcu-independent transport of succinate in Escherichia coli : contribution of diffusion and of alternative carriers

2001

Quintuple mutants of Escherichia coli deficient in the C4-dicarboxylate carriers of aerobic and anaerobic metabolism (DctA, DcuA, DcuB, DcuC, and the DcuC homolog DcuD, or the citrate/succinate antiporter CitT) showed only poor growth on succinate (or other C4-dicarboxylates) under oxic conditions. At acidic pH (pH 6) the mutants regained aerobic growth on succinate, but not on fumarate. Succinate uptake by the mutants could not be saturated at physiological succinate concentrations (≤5 mM), in contrast to the wild-type, which had a K m for succinate of 50 µM and a V max of 35 U/g dry weight at pH 6. At high substrate concentrations, the mutants showed transport activities (32 U/g dry weigh…

AntiporterMutantSuccinic AcidBiologymedicine.disease_causeBiochemistryMicrobiologyBacterial ProteinsFumaratesNitrilesEscherichia coliGeneticsmedicineMolecular BiologyEscherichia coliDicarboxylic Acid TransportersUncoupling AgentsEscherichia coli ProteinsBiological TransportGeneral MedicineMetabolismHydrogen-Ion ConcentrationFumarate reductasebiology.organism_classificationEnterobacteriaceaeBiochemistryMutationFermentationEffluxCarrier ProteinsArchives of Microbiology
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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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