Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS.
The hydrophobin EAS from the fungus Neurospora crassa forms functional amyloid fibrils called rodlets that facilitate spore formation and dispersal. Self-assembly of EAS into fibrillar rodlets occurs spontaneously at hydrophobic:hydrophilic interfaces and the rodlets further associate laterally to form amphipathic monolayers. We have used site-directed mutagenesis and peptide experiments to identify the region of EAS that drives intermolecular association and formation of the cross-β rodlet structure. Transplanting this region into a nonamyloidogenic hydrophobin enables it to form rodlets. We have also determined the structure and dynamics of an EAS variant with reduced rodlet-forming ability. Taken together, these data allow us to pinpoint the conformational changes that take place when hydrophobins self-assemble at an interface and to propose a model for the amphipathic EAS rodlet structure.
School of Molecular Bioscience, University of Sydney, Sydney, New South Wales 2006, Australia.
Ingrid
I
Macindoe
Ann H
AH
Kwan
Qin
Q
Ren
Vanessa K
VK
Morris
Wenrong
W
Yang
Joel P
JP
Mackay
Margaret
M
Sunde
D000595:Amino Acid Sequence; D000682:Amyloid / Q000378:metabolism*; D005658:Fungi / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D046529:Microscopy, Electron, Transmission; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D017386:Sequence Homology, Amino Acid
D000682:Amyloid