Open AccessThe N ‐terminal domain of the Flo11 protein from S accharomyces cerevisiae is an adhesin without mannose‐binding activity
Author(s) -
Goossens Katty V.Y.,
Willaert Ronnie G.
Publication year - 2012
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1111/j.1567-1364.2011.00766.x
Subject(s) - saccharomyces cerevisiae , mannose , biology , biochemistry , surface plasmon resonance , binding domain , peptide sequence , biophysics , microbiology and biotechnology , binding site , gene , materials science , nanoparticle , nanotechnology
The expression of the Flo11 flocculin in S accharomyces cerevisiae offers the cell a wide range of phenotypes, depending on the strain and the environmental conditions. The most important are pseudohyphae development, invasive growth and flocculation. The mechanism of cellular adhesion mediated by Flo11p is not well understood. Therefore, the N ‐terminal domain of Flo11p was purified and studied. Although its amino acid sequence shows less similarity with the other flocculins, Flo11p belongs to the flocculin family. However, the N ‐terminal domain contains the ‘ Flo11 ‐domain’ ( PF 10181), but not the mannose‐binding PA 14 domain, which is present in the other flocculins ( Flo1p , Flo5p , Flo9p and Flo10p ). Structural and binding properties of the N ‐terminal domain of Flo11p were studied. It is shown that this domain is O ‐glycosylated and is structurally composed mainly of β‐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, surface plasmon resonance analysis showed that N‐Flo11p self‐interacts and explains the cell–cell interaction capacity of FLO11 ‐expressing cells.