Search results for "wall"

showing 10 items of 970 documents

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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Role of Pir1 in the construction of the Candida albicans cell wall

2004

Searches in a Candida albicans database (http://genolist.pasteur.fr/CandidaDB/) identified two Individual Protein Files (IPF 15363 and 19968) whose deduced amino acid sequences showed 42 % and 45 % homology with Saccharomyces cerevisiae Pir4. The two DNA sequences are alleles of the same gene (CaPIR1) but IPF 19968 has a deletion of 117 bases. IPF 19968 encodes a putative polypeptide of 364 aa, which is highly O-glycosylated and has an N-mannosylated chain, four cysteine residues and seven repeats. Both alleles are expressed under different growth conditions and during wall construction by regenerating protoplasts. The heterozygous mutant cells are elongated, form clumps of several cells an…

Saccharomyces cerevisiae Proteinsbeta-GlucansSequence Homology Amino AcidSaccharomyces cerevisiaeNucleic acid sequenceSaccharomyces cerevisiaeBiologybiology.organism_classificationMicrobiologyHomology (biology)EpitopeCorpus albicansFungal ProteinsBiochemistryCell WallCandida albicansAmino Acid SequenceCandida albicansGenePeptide sequenceGlycoproteins
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Molecular cloning and characterization of a Candida albicans gene coding for cytochrome c haem lyase and a cell wall-related protein.

1998

Immunoscreening of a Candida albicans cDNA library with a monoclonal antibody (mAb 4C12) recognizing an epitope present in high-molecular-weight mannoprotein (HMWM) components specific for the mycelial cell walls (a 180 kDa component and a polydispersed 260 kDa species) resulted in the isolation of the gene CaCYC3 encoding for cytochrome c haem lyase (CCHL). The CaCYC3 gene was transcribed preferentially in mycelial cells in which two mRNA transcripts of 0.8 and 1 kb were found. The nucleotide and the deduced amino acid sequences of this gene displayed 45% homology and 46% identity, respectively, to the Saccharomyces cerevisiae CYC3 gene and shared common features with other reported genes …

Saccharomyces cerevisiaeBlotting WesternGenes FungalMolecular Sequence DataFluorescent Antibody TechniqueLyasesSaccharomyces cerevisiaeMolecular cloningMicrobiologyHomology (biology)Fungal ProteinsCell WallImmunoscreeningSequence Homology Nucleic AcidCandida albicansAmino Acid SequenceRNA MessengerCloning MolecularCandida albicansMolecular BiologyGeneMembrane GlycoproteinsbiologyBase SequencecDNA libraryRNA FungalSequence Analysis DNALyasebiology.organism_classificationBlotting NorthernMolecular biologyMitochondriaBiochemistrySequence AlignmentMolecular microbiology
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Starvation and temperature upshift cause an increase in the enzymatically active cell wall-associated glyceraldehyde-3-phosphate dehydrogenase protei…

2003

The cell wall-associated glyceraldehyde-3-phosphate dehydrogenase (cwGAPDH) activity in Saccharomyces cerevisiae increases (two- to 10-fold, depending on the strain) in response to starvation and temperature upshift. Assays using transformants carrying pTDH, a yeast centromer derivative plasmid containing the Candida albicans TDH3 gene (encoding GAPDH) fused in frame with the yeast SUC2-coding region for internal invertase, showed that starvation and/or temperature upshift result in a similar increase in both cwGAPDH and cell wall-associated invertase activities. In addition, this incorporation of GAPDH protein into the cell wall in response to stress does not require (i) de novo protein sy…

Saccharomyces cerevisiaeDehydrogenaseSaccharomyces cerevisiaeBiologyApplied Microbiology and BiotechnologyMicrobiologyFungal ProteinsCell WallGene Expression Regulation FungalCandida albicansCandida albicansGlyceraldehyde 3-phosphate dehydrogenasechemistry.chemical_classificationTemperatureGlyceraldehyde-3-Phosphate DehydrogenasesGeneral Medicinebiology.organism_classificationMolecular biologyYeastCytosolEnzymeInvertasechemistryBiochemistryStarvationbiology.proteinFEMS Yeast Research
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PATRIMONIO MILITARE E PROGETTI DI RIGENERAZIONE URBANA. L’INFRASTRUTTURA BELLICA DELL’ATLANTIC WALL E DI SAINT-NAZAIRE

2013

Nel 2010, la base sottomarina di Saint-Nazaire è stata dichiarata «patrimonio del XX secolo» dal Ministère de la Culture et de la Communnication francese ed è divenuta il simbolo di un nuovo approccio patrimoniale che riconosce il patrimonio materiale e immateriale in tutte le sue forme, non limitandosi soltanto al manufatto certificato come monumento. La memoria, i beni materiali o i luoghi poco conosciuti possono così contribuire a definire una nuova dimensione urbana, che si relaziona al futuro. Riferirsi esplicitamente al tema del rapporto tra waterfornt e patrimoinio militare, attraverso l’esempio di Saint-Nazaire, ci porta a riflettere sul ruolo del progetto urbano nella trasformazion…

Saint-Nazaire city harbour military heritage Atlantic WallSettore ICAR/14 - Composizione Architettonica E UrbanaSaint-Nazaire città porto bunker patrimonio militare Atlantic WallHeritage Saint-Nazaire Port citiesU-Boat Bases
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