6533b828fe1ef96bd1288dc1
RESEARCH PRODUCT
Identification and study of a Candida albicans protein homologous to Saccharomyces cerevisiae Ssr1p, an internal cell-wall protein
Ana I. MartínezLuis CastilloEulogio ValentínAna GarceraRafael SentandreuM. Victoria Elorzasubject
Signal peptideSaccharomyces cerevisiae ProteinsMolecular Sequence DataSaccharomyces cerevisiaeGene ExpressionSaccharomyces cerevisiaeCalcofluor-whiteMicrobiologyFungal ProteinsCell wallSpecies SpecificityCell WallCandida albicansAmino Acid SequenceCloning MolecularDNA FungalCandida albicansGenePeptide sequencechemistry.chemical_classificationBase SequenceSequence Homology Amino Acidbiologybiology.organism_classificationAmino acidBiochemistrychemistryGene Deletiondescription
After screening of aCandida albicansgenome database, the product of an ORF (IPF 3054) that has 62 % homology withSaccharomyces cerevisiaeSsr1p, an internal cell-wall protein, was identified and named CaSsr1p. The deduced amino acid sequence shows that CaSsr1p contains an N-terminal hydrophobic signal peptide, is rich in Ser and Thr amino acids and has a potential glycosylphosphatidylinositol-attachment signal. CaSsr1p is released following degradation of isolated cell walls by zymolyase (mainly a 1,3-β-glucanase) and therefore seems to be covalently linked to theβ-glucan of the cell walls. Both disruption and overexpression of theCaSSR1gene caused an increased sensitivity to calcofluor white, Congo red and zymolyase digestion. These results suggest that CaSsr1p has a structural role associated with the cell-wallβ-glucan.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2003-08-01 | Microbiology |