engleski

Effect of the BGL2 mutation on properties of the yeast cell wall

Saccharomyces cerevisiae cell wall is composed of an inner glucan layer, and of an outer mannoprotein sheath. Cell wall mannoproteins can be non-covalently or covalently linked to the cell wall. Non-covalent interactions between the glucan layer and mannoproteins occur through protein parts of mannoproteins while the covalent linkage occurs between glucan and mannan moiety of mannoproteins. It has been reported that the BGL2 gene product, a cell wall endoglucanase, might have a role in glucan assembly in the yeast cell wall. Since the glucan assembly could affect protein anchoring and architecture of the cell wall, we attempted to asses differences in the cell wall protein anchoring between the S. cerevisiae mutant strain which lacks BGL2 gene, and his parental wild type. Therefore, the level of covalently and non-covalently linked proteins in the cell walls of those two strains has been measured. Besides, the effect of such mutation on protein and DNA transport through the cell wall has been analyzed. Results showed that the mutation of the BGL2 gene decreased the level of cross-linking between mannan and glucan and increased the DNA uptake into the cell. At the same time the protein uptake was decreased, as well as the sensitivity of the cell wall to the Zymolyase treatment.

Saccharomyces cerevisiae; cell wall; cell wall proteins; BGL2

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