0000000000281104

AUTHOR

Mercedes Montero

showing 3 related works from this author

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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A Candida albicans 37 kDa polypeptide with homology to the laminin receptor is a component of the translational machinery.

1998

A cDNA encoding a 37 kDa protein was isolated from an expression library using antibodies raised against mycelial cell walls fromCandida albicans.The 37 kDa protein has over 60% sequence identity with the 37 kDa laminin-binding protein (LBP) from humans and over 80% identity with the Yst proteins ofSaccharomyces cerevisiae. TheC. albicansprotein was named CaYst1. It was found in membrane and ribosome fractions but surprisingly, was not found in cell walls. Unlike the human LBP, CaYst1p does not bind laminin. These data indicate that CaYst1p is not a cell-surface receptor for laminin as has been proposed for the human LBP. Instead, like theS. cerevisiaeYst proteins, it appears to be a riboso…

Ribosomal ProteinsSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeBlotting WesternMolecular Sequence DataMicrobiologyFungal ProteinsReceptors LamininRibosomal proteinComplementary DNACandida albicansAnimalsHumansCandida albicansAntibodies Fungalchemistry.chemical_classificationFungal proteinbiologyBase SequenceBinding proteinMembrane Proteinsbiology.organism_classificationBlotting NorthernMolecular biologyBlotting SouthernCytoskeletal ProteinsBiochemistrychemistryMembrane proteinProtein BiosynthesisRabbitsGlycoproteinSequence AlignmentMicrobiology (Reading, England)
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Yarrowia lipolytica cell wall architecture: interaction of Ywp1, a mycelial protein, with other wall components and the effect of its depletion

1999

Linkages of Ywp1 to other components of the Yarrowia lipolytica mycelial cell wall were studied by extraction with beta-mercaptoethanol and zymolyase (a beta-glucanase complex) and by the use of rabbit polyclonal antibody preparation raised against Ywp1. Ywp1 complexed with an N-glycosylated cell wall protein(s) to form supramolecular complexes through disulphide bridges (extractable with beta-mercaptoethanol) or bonded to beta-1,3-glucan (extractable with zymolyase). The lack of a specific morphological phenotype when YWP1 was knocked out by gene disruption might indicate that other proteins present in the cell wall of Y. lipolytica compensated for its loss. In this mutant, the electrophor…

Microscopy ConfocalbiologyBlotting WesternMutantYarrowiaGeneral MedicineCalcofluor-whitebiology.organism_classificationMicrobiologyWheat germ agglutininFungal ProteinsCell wallchemistry.chemical_compoundPhenotypeBiochemistryChitinchemistryCell WallPolyclonal antibodiesSaccharomycetalesChitinasebiology.proteinAnimalsRabbitsMolecular BiologyResearch in Microbiology
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