Novel Hydrophobins from Trichoderma Define a New Hydrophobin Subclass: Protein Properties, Evolution, Regulation and Processing
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Hydrophobins are small proteins, characterised by the presence of eight positionally conserved cysteine residues, and are present in all filamentous asco- and basidiomycetes. They are found on the outer surfaces of cell walls of hyphae and conidia, where they mediate interactions between the fungus and the environment. Hydrophobins are conventionally grouped into two classes (class I and II) according to their solubility in solvents, hydropathy profiles and spacing between the conserved cysteines. Here we describe a novel set of hydrophobins from Trichoderma spp. that deviate from this classification in their hydropathy, cysteine spacing and protein surface pattern. Phylogenetic analysis shows that they form separate clades within ascomycete class I hydrophobins. Using T. atroviride as a model, the novel hydrophobins were found to be expressed under conditions of glucose limitation and to be regulated by differential splicing.
KeywordsHydrophobin Trichoderma Protein evolution Protein processing Peptidomics Splicing Hypocrea
This study was supported by the Fifth (EC) Framework program (Quality of Life and Management of Living Resources; Project EUROFUNG 2; QLK3-1999-00729) to CPK and HVD, by the FWF Austrian Science Fund (P-19690 to CPK and T390 to VS) and by a fellowship from the Deutsche Forschungsgemeinschaft (Do270/10) to HVD. The work conducted by the U.S. Department of Energy Joint Genome Institute is supported by the Office of Science of the U.S. Department of Energy under Contract No. DE-AC02-05CH11231. SEB was supported by the DOE EERE Office of the Biomass Program.
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