The Filament-specific Rep1-1 Repellent of the Phytopathogen Ustilago maydis Forms Functional Surface-active Amyloid-like Fibrils

Repellents of the maize pathogen Ustilago maydis are involved in formation of hydrophobic aerial hyphae and in cellular attachment. These peptides, called Rep1-1 to Rep1-11, are encoded by the rep1 gene and result from cleavage of the precursor protein Rep1 during passage of the secretion pathway. U...

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Published in:	The Journal of biological chemistry 2009-04, Vol.284 (14), p.9153-9159
Main Authors:	Teertstra, Wieke R., van der Velden, Gisela J., de Jong, Jan F., Kruijtzer, John A.W., Liskamp, Rob M.J., Kroon-Batenburg, Loes M.J., Müller, Wally H., Gebbink, Martijn F.B.G., Wösten, Han A.B.
Format:	Article
Language:	eng
Subjects:	Amyloid - genetics Amyloid - metabolism Fungal Proteins - genetics Fungal Proteins - metabolism Gene Expression Regulation, Fungal Microscopy, Electron Molecular Basis of Cell and Developmental Biology Peptide Fragments - genetics Peptide Fragments - metabolism Ustilago - genetics Ustilago - metabolism Ustilago - pathogenicity Ustilago - ultrastructure Ustilago maydis Zea mays
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Summary:	Repellents of the maize pathogen Ustilago maydis are involved in formation of hydrophobic aerial hyphae and in cellular attachment. These peptides, called Rep1-1 to Rep1-11, are encoded by the rep1 gene and result from cleavage of the precursor protein Rep1 during passage of the secretion pathway. Using green fluorescent protein as a reporter, we here show that rep1 is expressed in filaments and not in the yeast form of U. maydis. In situ hybridization localized rep1 mRNA in the apex of the filament, which correlates with the expected site of secretion of the repellents into the cell wall. We also produced a synthetic peptide, Rep1-1. This peptide reduced the water surface tension to as low as 36 mJ m-2. In addition, it formed amyloid-like fibrils as was shown by negative staining, by thioflavin T fluorescence, and by x-ray diffraction. These fibrils were not soluble in SDS but could be dissociated with trifluoroacetic acid. The repellents in the hyphal cell wall had a similar solubility and also stained with thioflavin T, strongly indicating that they are present as amyloid fibrils. However, such fibrils could not be observed at the hyphal surface. This can be explained by the fact that the Rep1-1 filaments decrease in length at increasing concentrations. Taken together, we have identified the second class of fungal proteins that form functional amyloid-like filaments at the hyphal surface.
ISSN:	0021-9258 1083-351X