1887

Abstract

After screening of a genome database, the product of an ORF (IPF 3054) that has 62 % homology with Ssr1p, 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--glucanase) and therefore seems to be covalently linked to the -glucan of the cell walls. Both disruption and overexpression of the gene 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-wall -glucan.

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2003-08-01
2020-10-27
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