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THE PLANT CELL, Vol 5, Issue 11 1567-1574, Copyright © 1993 by American Society of Plant Biologists
Interfacial Self-Assembly of a Fungal Hydrophobin into a Hydrophobic Rodlet Layer
HAB. Wosten, OMH. de Vries and JGH. Wessels
Department of Plant Biology, Biological Centre, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands
The Sc3p hydrophobin of the basidiomycete Schizophyllum commune is a small
hydrophobic protein (100 to 101 amino acids) containing eight cysteine
residues. Large amounts of the protein are excreted into the culture medium
as monomers, but in the walls of aerial hyphae, the protein is present as
an SDS-insoluble complex. In this study, we show that the Sc3p hydrophobin
spontaneously assembles into an SDS-insoluble protein membrane on the
surface of gas bubbles or when dried down on a hydrophilic surface.
Electron microscopy of the assembled hydrophobin shows a surface consisting
of rodlets spaced 10 nm apart, which is similar to those rodlets seen on
the surface of aerial hyphae. When the purified Sc3p hydrophobin assembles
on a hydrophilic surface, a surface is exposed with high hydrophobicity,
similar to that of aerial hyphae. The rodlet layer, assembled in vivo and
in vitro, can be disassembled by dissolution in trifluoroacetic acid and,
after removal of the acid, reassembled into a rodlet layer. We propose,
therefore, that the hydrophobic rodlet layer on aerial hyphae arises by
interfacial self-assembly of Sc3p hydrophobin monomers, involving
noncovalent interactions only. Submerged hyphae merely excrete monomers
because these hyphae are not exposed to a water-air interface. The
generally observed rodlet layers on fungal spores may arise in a similar
way.
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