title: Interfacial self-assembly of fungal hydrophobins of the lichen-forming ascomycetes Xanthoria parietina and X. ectaneoides.
abstract: In the symbiotic phenotype of the lichen-forming ascomycetes Xanthoria parietina and X. ectaneoides, a conglutinate, hydrophilic cortex surrounds a system of aerial hyphae with hydrophobic wall surfaces. In X. parietina freeze-fracture electron microscopy showed that a rodlet layer covers the fungal and algal wall surfaces. Extracts of hot SDS-insoluble wall residues isolated from both species contained a protein that revealed a rodlet layer upon interfacial self-assembly. The N-terminal sequence of the 10-kDa protein of X. ectaneoides served to clone cDNA fragments of XEH1 (H1 of X. ectaneoides) and XPH1 (H1 of X. parietina) by RT-PCR. Genomic DNA blot analysis with both lichenized species and the aposymbiotically cultured symbionts of X. parietina showed that XPH1 and XEH1 are fungal single copy genes. The deduced amino acid sequences of the two encoded proteins were 96% identical and showed the characteristics of class I hydrophobins.
authors.affiliation: Institute of Plant Biology, University of Zürich, Switzerland.
authors.forename: S
authors.initials: S
authors.lastname: Scherrer
authors.forename: O M
authors.initials: OM
authors.lastname: De Vries
authors.forename: R
authors.initials: R
authors.lastname: Dudler
authors.forename: J G
authors.initials: JG
authors.lastname: Wessels
authors.forename: R
authors.initials: R
authors.lastname: Honegger
mesh_terms: D000595:Amino Acid Sequence; D001203:Ascomycota / Q000145:classification / Q000235:genetics / Q000502:physiology* / Q000648:ultrastructure; D001483:Base Sequence; D003001:Cloning, Molecular; D005614:Freeze Fracturing / Q000379:methods; D005656:Fungal Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D008011:Lichens / Q000502:physiology*; D008854:Microscopy, Electron; D008969:Molecular Sequence Data; D017422:Sequence Analysis, DNA; D013559:Symbiosis
chemical_list: D005656:Fungal Proteins