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Novel hydrophobins from Trichoderma define a new hydrophobin subclass: protein properties, evolution, regulation and processing.

Journal Article · · Journal of Molecular Evolution
 [1]; ;  [2];  [3];  [2];  [3];  [4];  [5];  [6]
  1. Institute of Chemical Engineering, TU Wien, Vienna, Austria
  2. Sabanci University
  3. Anagnostec GmbH
  4. Technische Universitaet Berlin
  5. BATTELLE (PACIFIC NW LAB)
  6. Technische Universitat Wien
+ Show Author Affiliations
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.
Research Organization:
Pacific Northwest National Laboratory (PNNL), Richland, WA (United States)
Sponsoring Organization:
USDOE
DOE Contract Number:
AC05-76RL01830
OSTI ID:
1592701
Report Number(s):
PNNL-SA-80050
Journal Information:
Journal of Molecular Evolution, Journal Name: Journal of Molecular Evolution Journal Issue: 4 Vol. 72
Country of Publication:
United States
Language:
English

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Related Subjects

Fungi
hydrophobin