1887

Abstract

Pst1p was previously identified as a protein secreted by yeast regenerating protoplasts, which suggests a role in cell wall construction. encodes a protein homologous to Pst1p, and both of them display typical features of GPI-anchored proteins and a characteristic receptor L-domain. Pst1p and Ecm33p are both localized to the cell surface, Pst1p being at the cell membrane and possibly also in the periplasmic space. Here, the characterization of Δ, Δ and Δ Δ mutants is described. Deletion of leads to a weakened cell wall, and this defect is further aggravated by simultaneous deletion of . As a result, the Δ mutant displays increased levels of activated Slt2p, the MAP kinase of the cell integrity pathway, and relies on a functional Slt2-mediated cell integrity pathway to ensure viability. Analyses of model glycosylated proteins show glycosylation defects in the Δ mutant. Ecm33p is also important for proper cell wall ultrastructure organization and, furthermore, for the correct assembly of the mannoprotein outer layer of the cell wall. Pst1p seems to act in the compensatory mechanism activated upon cell wall damage and, in these conditions, may partially substitute for Ecm33p.

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2004-12-01
2019-11-19
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