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Volume 152, Issue 12

Repellents have functionally replaced hydrophobins in mediating attachment to a hydrophobic surface and in formation of hydrophobic aerial hyphae in Free

Abstract

contains one repellent and two class I hydrophobin genes in its genome. The repellent gene has been described previously. It encodes 11 secreted repellent peptides that result from the cleavage of a precursor protein at KEX2 recognition sites. The hydrophobin gene encodes a typical class I hydrophobin of 117 aa, while encodes a hydrophobin that is preceded by 17 repeat sequences. These repeats are separated, like the repellent peptides, by KEX2 recognition sites. Gene , but not , was shown to be expressed in a cross of two compatible wild-type strains, suggesting a role of the former hydrophobin gene in aerial hyphae formation. Indeed, aerial hyphae formation was reduced in a Δ cross. However, the reduction in aerial hyphae formation was much more dramatic in the Δ cross. Moreover, colonies of the Δ cross were completely wettable, while surface hydrophobicity was unaffected and only slightly reduced in the Δ and the ΔΔ cross, respectively. It was also shown that the repellents and not the hydrophobins are involved in attachment of hyphae to hydrophobic Teflon. Deleting either or both hydrophobin genes in the Δ strains did not further affect aerial hyphae formation, surface hydrophobicity and attachment. From these data it is concluded that hydrophobins of have been functionally replaced, at least partially, by repellents.

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2006-12-01
2024-04-16
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Repellents have functionally replaced hydrophobins in mediating attachment to a hydrophobic surface and in formation of hydrophobic aerial hyphae in Ustilago maydis
Microbiology 152, 3607 (2006); https://doi.org/10.1099/mic.0.29034-0
/content/journal/micro/10.1099/mic.0.29034-0
/content/journal/micro/10.1099/mic.0.29034-0
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