Hydrophobin

Hydrophobins are a class of small, cysteine rich proteins (~ 100 amino acids) that are expressed only by filamentous fungi. They are known for their capability of forming a hydrophobic (water-repellent) coating on a surface of an object.^[1] They were first discovered and separated in Schizophyllum commune in 1991. Based on differences in hydropathy patterns and biophysical properties, they are divided into two categories: class I and class II. Hydrophobins can self-assemble into monolayer on hydrophobic:hydrophilic interfaces, such as water:air interface. Class I monolayer contains the same core structure as amyloid fibrils, which is positive to Congo red and thioflavin T. Monolayer formed by class I hydrophobins has highly ordered structure, and they can only be dissociated by neat trifluoroacetate or formic acid.

Fungi make complex aerial structures and spores even in aqueous environments.

Hydrophobins have been identified in ascomycetes and basidiomycetes; whether they exist in other groups is not known.^[2] Hydrophobins are generally found on the outer surface of conidia and of the hyphal wall, and may be involved in mediating contact and communication between the fungus and its environment.^[3] Some family members contain multiple copies of the domain.

This family of poteins includes the rodlet proteins of Neurospora crassa (gene eas) and Emericella nidulans (gene rodA), these proteins are the main component of the hydrophobic sheath covering the surface of many fungal spores.^[4][5]

References

Further reading

This article incorporates text from the public domain Pfam and InterPro IPR001338