The dual role of amyloid β-sheet interaction sequences in the cell surface properties of < i > FLO11 < /i > -encoded flocculins in the yeast < i > Saccharomyces cerevisiae < /i >

In this report, we show that flocculins encoded byFLO11 inSaccharomyces cerevisiae behave like adhesins inC. albicans. To do so, we show that the formation of nanodomains under an external physical force requires a threshold number of amyloid-forming sequences in the Flo11 protein. Then, using a genome editing approach, we constructed strains expressing variants of the Flo11 protein under the endogenous FLO11 promoter, leading to the demonstration that the loss of amyloid-forming sequences strongly reduces cell-cell interaction but has no effect on either plastic adherence or invasive growth in agar, both phenotypes being dependent on the N- and C-terminal ends of Flo11p. Finally, we show that the location of Flo11 is not altered either by the absence of amyloid-forming sequences or by the removal of the N- or C-terminus of the protein.
Source: eLife - Category: Biomedical Science Tags: Genetics and Genomics Source Type: research