The expression of the Flo11 flocculin in S. cerevisiae offers the cell a wide range of phenotypes, depending on the strain and the environmental conditions. The most important among them are pseudohyphae development, invasive growth and flocculation. The mechanism of cellular adhesion mediated by Flo11p is not well understood and therefore, the N-terminal domain of Flo11p was purified and studied. Although its amino acid sequence shows less similarity than the other flocculins, Flo11p belongs to the flocculin family. The overall domain structure of this cell wall protein is comparable to the other Flo proteins (Flo1p, Flo5p, Flo9p and Flo10p) and consists of an exposed N-terminal domain and a C-terminal domain including a GPI-anchor, separated by a central domain containing a highly repeated threonine- and serine-rich sequence. In this study, the characteristics and the binding properties of the N-terminal domain of Flo11p were studied. It was shown that this domain is O-glycosylated and is structurally composed mainly of ?-sheets, which is typical for the members of the flocculin family. Furthermore, fluorescence spectroscopy binding studies revealed that N-Flo11p does not bind mannose, which is in contrast to the other Flo proteins. However, SPR analysis showed that N-Flo11p self-interacts and explains the cell-cell interaction capacity of FLO11 expressing cells.
|Title of host publication||Yeasterday congres, Leiden University, Leiden, The Netherlands, May 20st, 2011|
|Publication status||Published - 20 May 2011|
|Event||Unknown - |
Duration: 20 May 2011 → …
|Period||20/05/11 → …|
- Saccharomyces cerevisiae