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Assembly of the fungal SC3 hydrophobin into functional amyloid fibrils depends on its concentration and is promoted by cell wall polysaccharides.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 2009 Sep 25; Vol. 284 (39), pp. 26309-14. Date of Electronic Publication: 2009 Aug 04. - Publication Year :
- 2009
-
Abstract
- Class I hydrophobins function in fungal growth and development by self-assembling at hydrophobic-hydrophilic interfaces into amyloid-like fibrils. SC3 of the mushroom-forming fungus Schizophyllum commune is the best studied class I hydrophobin. This protein spontaneously adopts the amyloid state at the water-air interface. In contrast, SC3 is arrested in an intermediate conformation at the interface between water and a hydrophobic solid such as polytetrafluoroethylene (PTFE; Teflon). This finding prompted us to study conditions that promote assembly of SC3 into amyloid fibrils. Here, we show that SC3 adopts the amyloid state at the water-PTFE interface at high concentration (300 microg ml(-1)) and prolonged incubation (16 h). Moreover, we show that amyloid formation at both the water-air and water-PTFE interfaces is promoted by the cell wall components schizophyllan (beta(1-3),beta(1-6)-glucan) and beta(1-3)-glucan. Hydrophobin concentration and cell wall polysaccharides thus contribute to the role of SC3 in formation of aerial hyphae and in hyphal attachment.
- Subjects :
- Amyloid chemistry
Cell Wall chemistry
Circular Dichroism
Electrophoresis, Polyacrylamide Gel
Fungal Proteins chemistry
Glucans chemistry
Glucans metabolism
Hydrophobic and Hydrophilic Interactions
Polysaccharides chemistry
Polytetrafluoroethylene chemistry
Protein Structure, Secondary
Water chemistry
Amyloid metabolism
Fungal Proteins metabolism
Polysaccharides metabolism
Schizophyllum metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1083-351X
- Volume :
- 284
- Issue :
- 39
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 19654326
- Full Text :
- https://doi.org/10.1074/jbc.M109.005553