Search results for "cell wall"

showing 10 items of 226 documents

Global transcriptional profiling ofCandida albicans cwt1 null mutant

2007

CaCwt1p is a Candida albicans putative transcriptional factor homologue to Rds2p in Saccharomyces cerevisiae. The lack of this protein in S. cerevisiae leads to a pleiotropic resistance to drugs and defects in cell wall architecture that are also detectable in C. albicans. It is also known that CaCwt1p is mainly expressed in the stationary growth phase of this fungus. In order to elucidate the role of CWT1, transcriptome analysis of the mutant strain was performed in exponential and stationary growth phases. A total of 460 genes were found to be up- or downregulated in the mutant strain growing exponentially, and 666 genes presented a misregulation when cwt1 cells reached the stationary pha…

ProteomeSaccharomyces cerevisiaeRibosome biogenesisBioengineeringApplied Microbiology and BiotechnologyBiochemistryFungal ProteinsTranscriptomeCell WallGene Expression Regulation FungalCandida albicansGeneticsPromoter Regions GeneticCandida albicansGeneTranscription factorOligonucleotide Array Sequence AnalysisBinding SitesbiologyCell growthGene Expression Profilingbiology.organism_classificationMolecular biologyProtein BiosynthesisMutationDNA microarrayGlycolysisTranscription FactorsBiotechnologyYeast
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Genomic response programs of Candida albicans following protoplasting and regeneration

2005

Transcription profiling of Candida albicans cells responding to the elimination of the wall (protoplasts) and posterior regeneration was explored. DNA microarrays were used to measure changes in the expression of 6039 genes, and the upregulated genes during regeneration at 28 degrees C were assigned to fourteen categories. A total of 407 genes were upregulated during the process, of which 144 reached a maximum after 1 h. MKC1, a gene encoding a member of the regulatory pathway involved in cell wall integrity was overexpressed. Time-dependent expression divided the genes into 40 clusters. Clusters 1-19 were highly expressed initially (time 0) and downregulated following incubation, whereas t…

Regulation of gene expressionbiologyGene Expression ProfilingProtoplastsbiology.organism_classificationMicrobiologyGenomeMolecular biologyFungal ProteinsGene expression profilingCell WallTranscription (biology)Gene Expression Regulation FungalCandida albicansGene expressionGeneticsCluster AnalysisRegenerationGenome FungalDNA microarrayCandida albicansGeneOligonucleotide Array Sequence AnalysisFungal Genetics and Biology
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Yeast karyopherins Kap123 and Kap95 are related to the function of the cell integrity pathway

2009

The characterization of mutant strains in the gene encoding karyopherin Kap123 has revealed several morphogenetic defects. Inactivation of KAP123 caused alterations in the actin cytoskeleton, resulting in hyperpolarization and resistance to the actin polymerization inhibitor latrunculin B. In fact, the level of actin filaments is increased in kap123 mutant cells. In addition to the defect in actin cytoskeleton, the kap123 mutant cells showed a weakened cell wall, cell lysis and a growth defect in either the presence of sodium dodecyl sulfate or at high temperatures, which is alleviated by osmotic stabilizers. These defects in cell integrity and the actin cytoskeleton suggested a relationshi…

Saccharomyces cerevisiae ProteinsArp2/3 complexMADS Domain ProteinsSaccharomyces cerevisiaemacromolecular substancesApplied Microbiology and BiotechnologyMicrobiologyGene Knockout TechniquesCell WallNuclear proteinCytoskeletonCytoskeletonProtein kinase CActinMicroscopyMicrobial ViabilitybiologyActin remodelingGeneral Medicinebeta KaryopherinsActin cytoskeletonActinsCell biologybiology.proteinLatrunculinMitogen-Activated Protein KinasesFEMS Yeast Research
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Physiological and genomic characterisation of Saccharomyces cerevisiae hybrids with improved fermentation performance and mannoprotein release capaci…

2015

Yeast mannoproteins contribute to several aspects of wine quality by protecting wine against protein haze, reducing astringency, retaining aroma compounds and stimulating lactic-acid bacteria growth. The selection of a yeast strain that simultaneously overproduces mannoproteins and presents good fermentative characteristics is a difficult task. In this work, a Saccharomyces cerevisiae × S. cerevisiae hybrid bearing the two oenologically relevant features was constructed. According to the genomic characterisation of the hybrids, different copy numbers of some genes probably related with these physiological features were detected. The hybrid shared not only a similar copy number of genes SPR1…

Saccharomyces cerevisiae ProteinsBiotecnología AgropecuariaSaccharomyces cerevisiaeGene DosageWineSaccharomyces cerevisiaeSPORE TO SPORE MATINGAliments MicrobiologiaMicrobiologyCell WallFermentacióHybridYEAST HYBRIDIZATIONMembrane Glycoproteinsbiologybusiness.industryGeneral MedicineHibridacióbiology.organism_classificationBiotechnologyYeast in winemakingCIENCIAS AGRÍCOLASRARE MATINGFermentationWINE YEASTBiotecnología Agrícola y Biotecnología AlimentariaHybridization GeneticFermentationChristian ministryGenome FungalbusinessFood ScienceInternational journal of food microbiology
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Response of the Saccharomyces cerevisiae Mpk1 Mitogen-Activated Protein Kinase Pathway to Increases in Internal Turgor Pressure Caused by Loss of Ppz…

2004

ABSTRACT The Mpk1 pathway of Saccharomyces cerevisiae is a key determinant of cell wall integrity. A genetic link between the Mpk1 kinase and the Ppz phosphatases has been reported, but the nature of this connection was unclear. Recently, the Ppz phosphatases were shown to be regulators of K + and pH homeostasis. Here, we demonstrate that Ppz-deficient strains display increased steady-state K + levels and sensitivity to increased KCl concentrations. Given these observations and the fact that K + is the major determinant of intracellular turgor pressure, we reasoned that the connection between PPZ1 and - 2 and MPK1 was due to the combination of increased internal turgor pressure in Ppz-defic…

Saccharomyces cerevisiae ProteinsGenotypeTranscription GeneticBlotting WesternTurgor pressureSaccharomyces cerevisiaePhosphataseSaccharomyces cerevisiaeMicrobiologyArticlePheromonesPotassium ChlorideCell wallPhosphoprotein PhosphatasesSorbitolPhosphorylationMolecular BiologyMembrane GlycoproteinsbiologyKinaseCalcium-Binding ProteinsIntracellular Signaling Peptides and ProteinsTemperatureMembrane ProteinsGeneral MedicineHydrogen-Ion ConcentrationBlotting Northernbiology.organism_classificationUp-RegulationPhenotypeBiochemistryMitogen-activated protein kinaseMutationPotassiumbiology.proteinPhosphorylationMitogen-Activated Protein KinasesIntracellularEukaryotic Cell
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Blockage of cell wall receptors for yeast killer toxin KT28 with antimannoprotein antibodies.

1990

Binding of yeast killer toxin KT28 to its primary cell wall receptor was specifically blocked with polyclonal antimannoprotein antibodies which masked all toxin-binding sites on the surface of sensitive yeast cells. By indirect immunofluorescence, it was shown that KT28 binds to the cell wall mannoprotein and that the toxin resistance of mannoprotein mutants (mnn) of Saccharomyces cerevisiae was due to a lack of killer toxin-binding sites within the yeast cell wall. Structural analysis of acetylated mannoprotein from KT28-resistant mutant strains identified the outer mannotriose side chains as the actual killer toxin-binding domains.

Saccharomyces cerevisiae ProteinsMutantSaccharomyces cerevisiaeFluorescent Antibody TechniqueSaccharomyces cerevisiaeBiologymedicine.disease_causeAntibodiesCell wallCell WallmedicinePharmacology (medical)ReceptorPharmacologyMembrane GlycoproteinsToxinMycotoxinsbiology.organism_classificationYeastKiller Factors YeastCell biologycarbohydrates (lipids)Infectious DiseasesBiochemistryPolyclonal antibodiesbiology.proteinAntibodyResearch Article
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Molecular structure of the cell wall receptor for killer toxin KT28 in Saccharomyces cerevisiae

1988

The adsorption of the yeast killer toxin KT28 to susceptible cells of Saccharomyces cerevisiae was prevented by concanavalin A, which blocks the mannoprotein receptor. Certain mannoprotein mutants of S. cerevisiae that lack definite structures in the mannan of their cell walls were found to be resistant to KT28, whereas the wild-type yeast from which the mutants were derived was susceptible. Isolated mannoprotein from a resistant mutant was unable to adsorb killer toxin. By comparing the resistances of different mannoprotein mutants, information about the molecular structure of the receptor was obtained. At least two mannose residues have to be present in the side chains of the outer chain …

Saccharomyces cerevisiae ProteinsMutantSaccharomyces cerevisiaeMannoseReceptors Cell Surfacechemical and pharmacologic phenomenaSaccharomyces cerevisiaeSpheroplastsMicrobiologyFungal Proteinschemistry.chemical_compoundCell WallConcanavalin AReceptorMolecular BiologyGlycoproteinsMannanMembrane GlycoproteinsbiologyMycotoxinsSpheroplastbiology.organism_classificationKiller Factors YeastYeastcarbohydrates (lipids)BiochemistrychemistryConcanavalin AMutationbiology.proteinAdsorptionResearch ArticleJournal of Bacteriology
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Mannoprotein of the yeast cell wall as primary receptor for the killer toxin of Saccharomyces cerevisiae strain 28.

1987

The killer toxin KT 28 of Saccharomyces cerevisiae strain 28 is primarily bound to the mannoprotein of the cell wall of sensitive yeasts. The mannoprotein of S. cerevisiae X 2180 was purified; gel filtration and SDS-PAGE indicated an estimated Mr of 185,000. The ability to bind killer toxin KT 28 increased during purification of the mannoprotein. Removing the protein part of the mannoprotein by enzymic digestion or removing the alkali-labile oligosaccharide chains by beta-elimination did not destroy the ability to bind killer toxin KT 28. However, binding activity was lost when the 1,6-alpha-linkages of the outer carbohydrate backbone were hydrolysed by acetolysis. The separated oligomannos…

Saccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiaeBiologymedicine.disease_causeMicrobiologyChromatography AffinityCell wallSepharoseAffinity chromatographyCell WallmedicineReceptorGlycoproteinschemistry.chemical_classificationMembrane GlycoproteinsToxinOligosaccharideMycotoxinsbiology.organism_classificationChromatography Ion ExchangeYeastKiller Factors Yeastcarbohydrates (lipids)chemistryBiochemistryAdsorptionJournal of general microbiology
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The ATC1 gene encodes a cell wall-linked acid trehalase required for growth on trehalose in Candida albicans.

2004

After screening a Candida albicans genome data base, the product of an open reading frame (IPF 19760/CA2574) with 41% identity to Saccharomyces cerevisiae vacuolar acid trehalase (Ath1p) was identified and named Atc1p. The deduced amino acid sequence shows that Atc1p contains an N-terminal hydrophobic signal peptide and 20 potential sites for N-glycosylation. C. albicans homozygous mutants that lack acid trehalase activity were constructed by gene disruption at the two ATC chromosomal alleles. Analysis of these null mutants shows that Atc1p is localized in the cell wall and is required for growth on trehalose as a carbon source. An Atc1p endowed with acid trehalase activity was obtained by …

Saccharomyces cerevisiae ProteinsTime FactorsTranscription GeneticMutantBlotting WesternMolecular Sequence DataTrehalase activityBiologyBiochemistrychemistry.chemical_compoundOpen Reading FramesCell WallCandida albicansAmino Acid SequenceRNA MessengerTrehalaseTrehalaseCandida albicansMolecular BiologyPeptide sequenceAlleleschemistry.chemical_classificationCell-Free SystemModels GeneticSequence Homology Amino AcidReverse Transcriptase Polymerase Chain ReactionStructural geneHomozygoteNuclear ProteinsTrehaloseCell BiologyDNAbiology.organism_classificationPhosphoproteinsTrehaloseCarbonAmino acidProtein Structure TertiaryGlucosechemistryBiochemistryProtein BiosynthesisMutationElectrophoresis Polyacrylamide GelCell DivisionPlasmidsThe Journal of biological chemistry
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Investigation of a Killer Strain of Zygosaccharomyces Bailii

1993

Summary: The yeast Zygosaccharomyces bailii strain 412 was found to liberate a killer toxin (KT412) lethal to sensitive strains of Saccharomyces cerevisiae and Candida glabrata. Culture supernatants of the killer strain were concentrated by ultrafiltration and the extracellular protein was purified by gel filtration and ion-exchange chromatography. Gel filtration and SDS-PAGE of the electrophoretically homogeneous killer protein indicated an apparent molecular mass of 10 kDa. The killer toxin KT412 is probably not glycosylated since it did not show any detectable carbohydrate structures. KT412 was bound to sensitive but not to resistant yeast cells. The mannan, and not the glucan, fraction …

Saccharomyces cerevisiae ProteinsZygosaccharomyces bailiiSaccharomyces cerevisiaechemical and pharmacologic phenomenaSaccharomyces cerevisiaeCycloheximideBiologymedicine.disease_causeMicrobiologyMicrobiologyMannanschemistry.chemical_compoundCell WallmedicineGlucansRNA Double-StrandedMannanGlucanchemistry.chemical_classificationMolecular massToxinRNA FungalMycotoxinsbiology.organism_classificationKiller Factors YeastYeastchemistryBiochemistrySaccharomycetalesJournal of General Microbiology
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