Hydrophobin
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Hydrophobin | ||||||||
| Pfam | PF01185 | ||||||||
| InterPro | IPR001338 | ||||||||
| PROSITE | PDOC00739 | ||||||||
| SCOP | 1r2m | ||||||||
| SUPERFAMILY | 1r2m | ||||||||
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| Structure of hydrophobin HFBI from Trichoderma reesei | |||||||||
| Identifiers | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Symbol | Hydrophobin_2 | ||||||||
| Pfam | PF06766 | ||||||||
| InterPro | IPR010636 | ||||||||
| PROSITE | PDOC00739 | ||||||||
| SCOP | 1r2m | ||||||||
| SUPERFAMILY | 1r2m | ||||||||
| OPM protein | 1r2m | ||||||||
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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 proteins 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]
[edit] References
- ^ Sunde M, Kwan AH, Templeton MD, Beever RE, Mackay JP (October 2008). "Structural analysis of hydrophobins". Micron 39 (7): 773–84. doi:10.1016/j.micron.2007.08.003. PMID 17875392.
- ^ Wösten (2001). "Hydrophobins: multipurpose proteins". Annual review of microbiology 55: 625–646. doi:10.1146/annurev.micro.55.1.625. PMID 11544369.
- ^ Whiteford JR, Spanu PD (2001). "The hydrophobin HCf-1 of Cladosporium fulvum is required for efficient water-mediated dispersal of conidia". Fungal Genet. Biol. 32 (3): 159–168. doi:10.1006/fgbi.2001.1263. PMID 11343402.
- ^ Stringer MA, Dean RA, Sewall TC, Timberlake WE (July 1991). "Rodletless, a new Aspergillus developmental mutant induced by directed gene inactivation". Genes Dev. 5 (7): 1161–71. PMID 2065971.
- ^ Lauter FR, Russo VE, Yanofsky C (December 1992). "Developmental and light regulation of eas, the structural gene for the rodlet protein of Neurospora". Genes Dev. 6 (12A): 2373–81. PMID 1459459.
[edit] Further reading
- Scholtmeijer K (2000). Expression and engineering of hydrophobin genes (Ph.D. thesis). University of Groningen. http://irs.ub.rug.nl/ppn/240088549.
- Hakanpää J, Paananen A, Askolin S, Nakari-Setälä T, Parkkinen T, Penttilä M, Linder MB, Rouvinen J (January 2004). "Atomic resolution structure of the HFBII hydrophobin, a self-assembling amphiphile". J. Biol. Chem. 279 (1): 534–9. doi:10.1074/jbc.M309650200. PMID 14555650.
- Wösten HA, de Vocht ML (September 2000). "Hydrophobins, the fungal coat unravelled". Biochim. Biophys. Acta 1469 (2): 79–86. doi:10.1016/S0304-4157(00)00002-2. PMID 10998570.
- Aimanianda V, Bayry J, Bozza S, Kniemeyer O, Perruccio K, Elluru SR, Clavaud C, Paris S, Brakhage AA, Kaveri SV, Romani L, Latgé JP (August 2009). "Surface hydrophobin prevents immune recognition of airborne fungal spores". Nature 460 (7259): 1117–21. doi:10.1038/nature08264. PMID 19713928.
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This article incorporates text from the public domain Pfam and InterPro IPR001338
