Structural highlights
Function
[RODL_NEUCR] Contributes to surface hydrophobicity, which is important for processes such as association of hyphae in reproductive structures, dispersal of aerial spores and adhesion of pathogens to host structures. Important for the formation of hydrophobic rodlet layers of asexually-produced spores.
Publication Abstract from PubMed
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-beta 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.
Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS.,Macindoe I, Kwan AH, Ren Q, Morris VK, Yang W, Mackay JP, Sunde M Proc Natl Acad Sci U S A. 2012 Apr 3;109(14):E804-11. Epub 2012 Jan 23. PMID:22308366[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Macindoe I, Kwan AH, Ren Q, Morris VK, Yang W, Mackay JP, Sunde M. Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS. Proc Natl Acad Sci U S A. 2012 Apr 3;109(14):E804-11. Epub 2012 Jan 23. PMID:22308366 doi:http://dx.doi.org/10.1073/pnas.1114052109
