title: Interactions by the Fungal Flo11 Adhesin Depend on a Fibronectin Type III-like Adhesin Domain Girdled by Aromatic Bands.
abstract: Saccharomyces cerevisiae harbors a family of GPI-anchored cell wall proteins for interaction with its environment. The flocculin Flo11, a major representative of these fungal adhesins, confers formation of different types of multicellular structures such as biofilms, flors, or filaments. To understand these environment-dependent growth phenotypes on a molecular level, we solved the crystal structure of the N-terminal Flo11A domain at 0.89-Å resolution. Besides a hydrophobic apical region, the Flo11A domain consists of a β sandwich of the fibronectin type III domain (FN3). We further show that homophilic Flo11-Flo11 interactions and heterophilic Flo11-plastic interactions solely depend on the Flo11A domain and are strongly pH dependent. These functions of Flo11A involve an apical region with its surface-exposed aromatic band, which is accompanied by acidic stretches. Together with electron microscopic reconstructions of yeast cell-cell contact sites, our data suggest that Flo11 acts as a spacer-like, pH-sensitive adhesin that resembles a membrane-tethered hydrophobin.
authors.affiliation: Department of Chemistry, Philipps-Universität, Hans-Meerwein-Straße 4, 35032 Marburg, Germany; Department of Biology, Philipps-Universität, Karl-von-Frisch-Straße 8, 35043 Marburg, Germany.
authors.forename: Timo
authors.initials: T
authors.lastname: Kraushaar
authors.affiliation: Department of Biology, Philipps-Universität, Karl-von-Frisch-Straße 8, 35043 Marburg, Germany.
authors.forename: Stefan
authors.initials: S
authors.lastname: Brückner
authors.affiliation: Department of Chemistry, Philipps-Universität, Hans-Meerwein-Straße 4, 35032 Marburg, Germany.
authors.forename: Maik
authors.initials: M
authors.lastname: Veelders
authors.affiliation: Department of Structural Biology, Max-Planck-Institute of Biophysics, Max-von-Laue-Straße 3, 60438 Frankfurt, Germany.
authors.forename: Daniel
authors.initials: D
authors.lastname: Rhinow
authors.affiliation: Department of Chemistry, Philipps-Universität, Hans-Meerwein-Straße 4, 35032 Marburg, Germany.
authors.forename: Franka
authors.initials: F
authors.lastname: Schreiner
authors.affiliation: Department of Biology, Philipps-Universität, Karl-von-Frisch-Straße 8, 35043 Marburg, Germany.
authors.forename: Raphael
authors.initials: R
authors.lastname: Birke
authors.affiliation: Department of Neuropathology, Philipps-Universität, Baldingerstraße 1, 35043 Marburg, Germany.
authors.forename: Axel
authors.initials: A
authors.lastname: Pagenstecher
authors.affiliation: Department of Biology, Philipps-Universität, Karl-von-Frisch-Straße 8, 35043 Marburg, Germany. Electronic address: moesch@staff.uni-marburg.de.
authors.forename: Hans-Ulrich
authors.initials: HU
authors.lastname: Mösch
authors.affiliation: Department of Chemistry, Philipps-Universität, Hans-Meerwein-Straße 4, 35032 Marburg, Germany; Department of Biology, Philipps-Universität, Karl-von-Frisch-Straße 8, 35043 Marburg, Germany. Electronic address: essen@chemie.uni-marburg.de.
authors.forename: Lars-Oliver
authors.initials: LO
authors.lastname: Essen
mesh_terms: D000595:Amino Acid Sequence; D024322:Amino Acids, Aromatic / Q000737:chemistry; D002448:Cell Adhesion / Q000502:physiology*; D005353:Fibronectins / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D005810:Multigene Family / Q000235:genetics*; D010802:Phylogeny; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000737:chemistry*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
chemical_list: D024322:Amino Acids, Aromatic; C110690:FLO11 protein, S cerevisiae; D005353:Fibronectins; D008562:Membrane Glycoproteins; D029701:Saccharomyces cerevisiae Proteins