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Published on: September 28, 2019
The hydrophobin EAS is largely unstructured in solution and functions by forming amyloid-like structures
J P Mackay1, J M Matthews, R D Winefield
1Department of Biochemistry, University of Sydney, NSW 2006, Sydney, Australia. j.mackay@biochem.usyd.edu.au
Fungal hydrophobins, like EAS protein, self-assemble into protective layers. This study reveals their amyloid-like structure, offering insights into their function and biotechnological potential.
Area of Science:
- Biochemistry
- Structural Biology
- Mycology
Background:
- Fungal hydrophobins form durable, amphipathic monolayers on aerial structures.
- These protein monolayers have potential biotechnological applications due to their surface polarity reversal capabilities.
- The molecular mechanisms of hydrophobin polymerization remain largely unknown.
Purpose of the Study:
- To investigate the structural basis of hydrophobin polymerization.
- To elucidate the molecular details of EAS (Epichloë/Aspergillus/Sordaria) hydrophobin assembly.
Main Methods:
- Purification of wild-type and 15N-labeled EAS from Neurospora crassa.
- Multidimensional NMR spectroscopy for high-resolution structural analysis.
- Analysis of Congo Red binding and birefringence for amyloid-like properties.
Main Results:
- EAS is monomeric and largely unstructured in solution, with a small beta-sheet region stabilized by disulfide bonds.
- Polymerized EAS exhibits increased beta-sheet content, resembling amyloid fibers.
- The protein displays characteristic gold-green birefringence with Congo Red.
Conclusions:
- EAS undergoes a disorder-to-order transition, a mechanism previously unlinked to its wild-type function.
- This study presents one of the few examples where an amyloid-like state is the functional wild-type form.
- Nature utilizes the amyloid formation mechanism for creating robust fungal structures.
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