Four conserved intramolecular disulphide linkages are required for secretion and cell wall localization of a hydrophobin during fungal morphogenesis.
Hydrophobins are morphogenetic proteins produced by fungi during assembly of aerial hyphae, sporulation, mushroom development and pathogenesis. Eight cysteine residues are present in hydrophobins and form intramolecular disulphide bonds. Here, we show that expressing eight cysteine-alanine substitution alleles of the MPG1 hydrophobin gene from Magnaporthe grisea causes severe defects in development of aerial hyphae and spores. Immunolocalization revealed that Mpg1 hydrophobin variants, lacking intact disulphide bonds, retain the capacity to self-assemble, but are not secreted to the cell surface. This provides the first genetic evidence that disulphide bridges in a hydrophobin are dispensable for aggregation, but essential for secretion.
Kershaw
Michael J
MJ
School of Biological Sciences, University of Exeter, Washington Singer Laboratories, Perry Road, Exeter EX4 4QG, UK.
Thornton
Christopher R
CR
Wakley
Gavin E
GE
Talbot
Nicholas J
NJ
D001203:Ascomycota / Q000235:genetics / Q000254:growth & development* / Q000378:metabolism / Q000472:pathogenicity; D002473:Cell Wall / Q000378:metabolism*; D003545:Cysteine; D004220:Disulfides / Q000737:chemistry*; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015966:Gene Expression Regulation, Fungal; D009024:Morphogenesis; D016297:Mutagenesis, Site-Directed; D012275:Oryza / Q000382:microbiology; D010935:Plant Diseases / Q000382:microbiology; D013172:Spores, Fungal / Q000254:growth & development
D004220:Disulfides; D005656:Fungal Proteins; D003545:Cysteine