Atomic composition of the hydrophobic and hydrophilic membrane sides of self-assembled SC3p hydrophobin.
The hydrophobin SC3p of Schizophyllum commune self-assembles into a 10-nm-thick amphipathic membrane at hydrophilic-hydrophobic interfaces. X-ray photoelectron spectroscopy of the hydrophobic membrane side of SC3p, assembled in vitro, showed an atomic composition similar to the calculated composition of SC3p when glycosylation was taken into account. The atomic composition measured at the hydrophilic membrane side deviated from that at the hydrophobic side and indicated the presence of a lower number of peptide bonds. High levels of S and N were detected only on mycelia carrying hydrophobic aerial hyphae, as expected with assembled SC3p present at the surface of these hyphae.
Department of Plant Biology, University of Groningen, Haren, The Netherlands.
H A
HA
Wösten
O M
OM
de Vries
H C
HC
van der Mei
H J
HJ
Busscher
J G
JG
Wessels
D005656:Fungal Proteins / Q000737:chemistry*; D006031:Glycosylation; D008567:Membranes, Artificial; D012567:Schizophyllum / Q000737:chemistry*; D013057:Spectrum Analysis; D014965:X-Rays
D005656:Fungal Proteins; D008567:Membranes, Artificial