Hydrophobin

Hydrophobin
Identifiers
Symbol Hydrophobin
Pfam PF01185
InterPro IPR001338
PROSITE PDOC00739
SCOP 1r2m
SUPERFAMILY 1r2m
Fungal hydrophobin

Structure of hydrophobin HFBI from Trichoderma reesei
Identifiers
Symbol Hydrophobin_2
Pfam PF06766
InterPro IPR010636
PROSITE PDOC00739
SCOP 1r2m
SUPERFAMILY 1r2m
OPM protein 1r2m

Hydrophobins are a group of small (~100 amino acids) cysteine-rich proteins that are expressed only by filamentous fungi. They are known for their ability to form a hydrophobic (water-repellent) coating on the surface of an object.[1] They were first discovered and separated in Schizophyllum commune in 1991.[2] Based on differences in hydropathy patterns and biophysical properties, they can be divided into two categories: class I and class II. Hydrophobins can self-assemble into a monolayer on hydrophobic:hydrophilic interfaces such as a water:air interface. Class I monolayer contains the same core structure as amyloid fibrils, and is positive to Congo red and thioflavin T. The monolayer formed by class I hydrophobins has a highly ordered structure, and can only be dissociated by concentrated trifluoroacetate or formic acid. Monolayer assembly involves large structural rearrangements with respect to the monomer.[3]

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.[4] 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.[5] 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.[6][7]

Genomic sequencing of two fungi from dry or salty environments (Wallemia sebi and W. ichthyophaga) revealed that these species contain predicted hydrophobins with unusually high proportion of acidic amino acids and therefore with potentially novel characteristics.[8] High proportion of acidic amino acids is thought to be an adaptation of proteins to high concentrations of salt.[9]

References

  1. ↑ 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.
  2. ↑ Wessels J, De Vries O, Asgeirsdottir SA, Schuren F (1991). "Hydrophobin Genes Involved in Formation of Aerial Hyphae and Fruit Bodies in Schizophyllum.". Plant Cell 3 (8): 793–799. doi:10.1105/tpc.3.8.793. PMC 160046. PMID 12324614.
  3. ↑ Morris V. K., Linser R., Wilde K. L., Duff A. P., Sunde M., Kwan A. H. (2012). "Solid-State NMR Spectroscopy of Functional Amyloid from a Fungal Hydrophobin: A Well-Ordered β-Sheet Core Amidst Structural Heterogeneity". Angew. Chem. Int. Ed. 51: 12621–12625. doi:10.1002/anie.201205625.
  4. ↑ Wösten (2001). "Hydrophobins: multipurpose proteins". Annual Review of Microbiology 55: 625–646. doi:10.1146/annurev.micro.55.1.625. PMID 11544369.
  5. ↑ 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.
  6. ↑ 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. doi:10.1101/gad.5.7.1161. PMID 2065971.
  7. ↑ 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. doi:10.1101/gad.6.12a.2373. PMID 1459459.
  8. ↑ Zajc, J.; Liu, Y.; Dai, W.; Yang, Z.; Hu, J.; Gostin Ar, C.; Gunde-Cimerman, N. (2013). "Genome and transcriptome sequencing of the halophilic fungus Wallemia ichthyophaga: Haloadaptations present and absent". BMC Genomics 14: 617. doi:10.1186/1471-2164-14-617. PMC 3849046. PMID 24034603.
  9. ↑ Madern, D.; Ebel, C.; Zaccai, G. (2000). "Halophilic adaptation of enzymes". Extremophiles : life under extreme conditions 4 (2): 91–98. doi:10.1007/s007920050142. PMID 10805563.

Further reading

  • Scholtmeijer K (2000). Expression and engineering of hydrophobin genes (Ph.D. thesis). University of Groningen. 
  • 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. 

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


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