Recruitment of class I hydrophobins to the air : water interface initiates a multi-step process of functional amyloid formation

Morris, Vanessa K., Ren, Qin, Macindoe, Ingrid, Kwan, Ann H., Byrne, Nolene and Sunde, Margaret 2011, Recruitment of class I hydrophobins to the air : water interface initiates a multi-step process of functional amyloid formation, Journal of biological chemistry, vol. 286, no. 18, pp. 15955-15963.

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Title Recruitment of class I hydrophobins to the air : water interface initiates a multi-step process of functional amyloid formation
Author(s) Morris, Vanessa K.
Ren, Qin
Macindoe, Ingrid
Kwan, Ann H.
Byrne, Nolene
Sunde, Margaret
Journal name Journal of biological chemistry
Volume number 286
Issue number 18
Start page 15955
End page 15963
Total pages 9
Publisher American Society for Biochemistry and Molecular Biology
Place of publication Bethesda, Md.
Publication date 2011-05-06
ISSN 0021-9258
1083-351X
Keyword(s) amyloid
fungi
protein conformation
protein self-assembly
protein structure
protein-protein interactions
Summary Class I fungal hydrophobins form amphipathic monolayers composed of amyloid rodlets. This is a remarkable case of functional amyloid formation in that a hydrophobic:hydrophilic interface is required to trigger the self-assembly of the proteins. The mechanism of rodlet formation and the role of the interface in this process have not been well understood. Here, we have studied the effect of a range of additives, including ionic liquids, alcohols, and detergents, on rodlet formation by two class I hydrophobins, EAS and DewA. Although the conformation of the hydrophobins in these different solutions is not altered, we observe that the rate of rodlet formation is slowed as the surface tension of the solution is decreased, regardless of the nature of the additive. These results suggest that interface properties are of critical importance for the recruitment, alignment, and structural rearrangement of the amphipathic hydrophobin monomers. This work gives insight into the forces that drive macromolecular assembly of this unique family of proteins and allows us to propose a three-stage model for the interface-driven formation of rodlets.
Language eng
Field of Research 039999 Chemical Sciences not elsewhere classified
Socio Economic Objective 970103 Expanding Knowledge in the Chemical Sciences
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2011, The American Society for Biochemistry and Molecular Biology, Inc.
Persistent URL http://hdl.handle.net/10536/DRO/DU:30040391

Document type: Journal Article
Collection: Centre for Material and Fibre Innovation
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