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J Biol Chem. 2009 Sep 25;284(39):26309-14. doi: 10.1074/jbc.M109.005553. Epub 2009 Aug 4.

Assembly of the fungal SC3 hydrophobin into functional amyloid fibrils depends on its concentration and is promoted by cell wall polysaccharides.

Author information

1
BioMaDe Technology, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands. K.Scholtmeijer@uu.nl

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.

PMID:
19654326
PMCID:
PMC2785318
DOI:
10.1074/jbc.M109.005553
[Indexed for MEDLINE]
Free PMC Article
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