Six hydrophobins are involved in hydrophobin rodlet formation in Aspergillus nidulans and contribute to hydrophobicity of the spore surface.
Hydrophobins are amphiphilic proteins able to self-assemble at water-air interphases and are only found in filamentous fungi. In Aspergillus nidulans two hydrophobins, RodA and DewA, have been characterized, which both localize on the conidiospore surface and contribute to its hydrophobicity. RodA is the constituent protein of very regularly arranged rodlets, 10 nm in diameter. Here we analyzed four more hydrophobins, DewB-E, in A. nidulans and found that all six hydrophobins contribute to the hydrophobic surface of the conidiospores but only deletion of rodA caused loss of the rodlet structure. Analysis of the rodlets in the dewB-E deletion strains with atomic force microscopy revealed that the rodlets appeared less robust. Expression of DewA and DewB driven from the rodA promoter and secreted with the RodA secretion signal in a strain lacking RodA, restored partly the hydrophobicity. DewA and B were able to form rodlets to some extent but never reached the rodlet structure of RodA. The rodlet-lacking rodA-deletion strain opens the possibility to systematically study rodlet formation of other natural or synthetic hydrophobins.
Karlsruhe Institute of Technology (KIT) - Campus South, Institute for Applied Biosciences (IAB), Department of Microbiology, Karlsruhe, Germany.
André
A
Grünbacher
Karlsruhe Institute of Technology (KIT) - Campus South, Institute for Applied Biosciences (IAB), Department of Microbiology, Karlsruhe, Germany.
Tanja
T
Throm
Karlsruhe Institute of Technology (KIT) - Campus South, Institute for Applied Biosciences (IAB), Department of Microbiology, Karlsruhe, Germany.
Constanze
C
Seidel
Karlsruhe Institute of Technology (KIT) - Campus South, Institute for Applied Biosciences (IAB), Department of Microbiology, Karlsruhe, Germany.
Beatrice
B
Gutt
Karlsruhe Institute of Technology (KIT) - Campus South, Institute for Applied Biosciences (IAB), Department of Microbiology, Karlsruhe, Germany.
Julian
J
Röhrig
KIT - Campus North, Institute of Nanotechnolgy (INT), Eggenstein-Leopoldshafen, Germany.
Timo
T
Strunk
KIT - Campus North, Institute of Applied Physics and INT, Eggenstein-Leopoldshafen, Germany.
Paul
P
Vincze
KIT - Campus North, Institute of Applied Physics and INT, Eggenstein-Leopoldshafen, Germany.
Stefan
S
Walheim
KIT - Campus North, Institute of Applied Physics and INT, Eggenstein-Leopoldshafen, Germany.
Thomas
T
Schimmel
KIT - Campus North, Institute of Nanotechnolgy (INT), Eggenstein-Leopoldshafen, Germany.
Wolfgang
W
Wenzel
Karlsruhe Institute of Technology (KIT) - Campus South, Institute for Applied Biosciences (IAB), Department of Microbiology, Karlsruhe, Germany.
Reinhard
R
Fischer
D000595:Amino Acid Sequence; D001233:Aspergillus nidulans / Q000235:genetics* / Q000378:metabolism; D005656:Fungal Proteins / Q000235:genetics* / Q000378:metabolism; D015966:Gene Expression Regulation, Fungal; D005816:Genetic Complementation Test; D057927:Hydrophobic and Hydrophilic Interactions; D018625:Microscopy, Atomic Force; D008969:Molecular Sequence Data; D020033:Protein Isoforms / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D013172:Spores, Fungal / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013499:Surface Properties
C095254:DEWA protein, Asperigillus nidulans; D005656:Fungal Proteins; D020033:Protein Isoforms