The N-terminal domain of the Flo11 protein from Saccharomyces cerevisiae is an adhesin without mannose binding activity

    Research output: Chapter in Book/Report/Conference proceedingMeeting abstract (Book)

    Abstract

    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.
    Original languageEnglish
    Title of host publicationYeasterday congres, Leiden University, Leiden, The Netherlands, May 20st, 2011
    Publication statusPublished - 20 May 2011
    EventUnknown -
    Duration: 20 May 2011 → …

    Conference

    ConferenceUnknown
    Period20/05/11 → …

    Keywords

    • Saccharomyces cerevisiae

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