The yeast cell wall, which for years has been regarded as a static cellular component, has been revealed to be dynamic in its structure and composition and complex in its enzymatic activity. The S. cerevisiae cell wall is composed of beta-1,3/beta-1,6-glucans, mannoproteins, and chitin, which are assembled into an extracellular matrix essential for maintenance of cell integrity. Gas1p, a glycoprotein anchored to the outer leaflet of the plasma membrane through a glycosylphosphatidylinositol, plays a key role in cell wall assembly. Loss of Gas1p leads to several morphogenetic defects and to a decrease in the amount of cross-links between the cell wall glucans. These defects in turn trigger a compensatory response that guarantees cell viability. Several Gas1p homologs have been isolated from Candida species and S. pombe. The Gas1p family also includes two plant proteins with endo-beta-1,3-glucanase activity. Sequence comparisons reveal that Gas1p family proteins have a modular organization of domains. The genetic and molecular analyses reviewed here suggest that Gas1p could play a role as a polymer cross-linker, presumably by catalyzing a transglycosylation reaction
Titolo: | The Gas1 glycoprotein, a putative wall polymer cross-linker |
Autori: | POPOLO, LAURA MARIA (Primo) |
Parole Chiave: | β-1,3-Glucanase; Glycoprotein; Glycosyl-phosphatidylinositol protein; Morphogenesis; Polymer cross-linking; Yeast cell wall |
Settore Scientifico Disciplinare: | Settore BIO/10 - Biochimica Settore BIO/11 - Biologia Molecolare |
Data di pubblicazione: | 1999 |
Rivista: | |
Tipologia: | Article (author) |
Digital Object Identifier (DOI): | 10.1016/S0304-4165(98)00138-X |
Appare nelle tipologie: | 01 - Articolo su periodico |