yang-selfassembly-2012.pdf (2.57 MB)
Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS
journal contributionposted on 2012-04-03, 00:00 authored by I Macindoe, A Kwan, Q Ren, V Morris, Wenrong YangWenrong Yang, J Mackay, M Sunde
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.
JournalNational Academy of Sciences. Proceedings
PublisherNational Academy of Sciences
LocationWashington, D. C.
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Publication classificationC1 Refereed article in a scholarly journal
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