title: Characterization of a Basidiomycota hydrophobin reveals the structural basis for a high-similarity Class I subdivision.
abstract: Class I hydrophobins are functional amyloids secreted by fungi. They self-assemble into organized films at interfaces producing structures that include cellular adhesion points and hydrophobic coatings. Here, we present the first structure and solution properties of a unique Class I protein sequence of Basidiomycota origin: the Schizophyllum commune hydrophobin SC16 (hyd1). While the core β-barrel structure and disulphide bridging characteristic of the hydrophobin family are conserved, its surface properties and secondary structure elements are reminiscent of both Class I and II hydrophobins. Sequence analyses of hydrophobins from 215 fungal species suggest this structure is largely applicable to a high-identity Basidiomycota Class I subdivision (IB). To validate this prediction, structural analysis of a comparatively distinct Class IB sequence from a different fungal order, namely the Phanerochaete carnosa PcaHyd1, indicates secondary structure properties similar to that of SC16. Together, these results form an experimental basis for a high-identity Class I subdivision and contribute to our understanding of functional amyloid formation.
authors.affiliation: Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, Canada.
authors.forename: Julie-Anne
authors.initials: JA
authors.lastname: Gandier
authors.affiliation: Department of Biochemistry &Molecular Biology, Dalhousie University, Halifax, Nova Scotia, Canada.
authors.forename: David N
authors.initials: DN
authors.lastname: Langelaan
authors.affiliation: Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada.
authors.forename: Amy
authors.initials: A
authors.lastname: Won
authors.affiliation: Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, Canada.
authors.forename: Kylie
authors.initials: K
authors.lastname: O'Donnell
authors.affiliation: Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, Canada.
authors.forename: Julie L
authors.initials: JL
authors.lastname: Grondin
authors.affiliation: Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, Canada.
authors.forename: Holly L
authors.initials: HL
authors.lastname: Spencer
authors.affiliation: e-Institute of Biomaterials and Biomedical Engineering, University of Toronto, Toronto, Ontario, Canada.
authors.forename: Philip
authors.initials: P
authors.lastname: Wong
authors.affiliation: e-Institute of Biomaterials and Biomedical Engineering, University of Toronto, Toronto, Ontario, Canada.
authors.forename: Elisabeth
authors.initials: E
authors.lastname: Tillier
authors.affiliation: Department of Medical Biophysics, University of Toronto, Toronto, Ontario, Canada.
authors.forename: Christopher
authors.initials: C
authors.lastname: Yip
authors.affiliation: Department of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, Canada.
authors.forename: Steven P
authors.initials: SP
authors.lastname: Smith
authors.affiliation: Department of Chemical Engineering and Applied Chemistry, University of Toronto, Toronto, Ontario, Canada.
authors.forename: Emma R
authors.initials: ER
authors.lastname: Master
mesh_terms: D000595:Amino Acid Sequence / Q000235:genetics; D000682:Amyloid / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure; D005656:Fungal Proteins / Q000737:chemistry* / Q000235:genetics / Q000648:ultrastructure; D006801:Humans; D018625:Microscopy, Atomic Force; D017433:Protein Structure, Secondary; D012567:Schizophyllum / Q000737:chemistry* / Q000235:genetics; D013499:Surface Properties; D014867:Water / Q000737:chemistry
chemical_list: D000682:Amyloid; D005656:Fungal Proteins; D014867:Water