De Ingeniis, Jessica and Raffaelli, Nadia and Ciani, Maurizio and Mannazzu, Ilaria Maria (2008) Pichia anomalaDBVPG 3003 secretes a ubiquitin-like protein that has antimicrobial activity. Applied and Environmental Microbiology, Vol. 75 (4), p. 1129-1134. eISSN 1098-5336. Article.
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The yeast strain Pichia anomala DBVPG 3003 secretes a killer toxin (Pikt) that has antifungal activity against Brettanomyces/Dekkera yeasts. Pikt interacts with β-1,6-glucan consistent with binding to the cell wall of the sensitive targets. In contrast to toxin K1 secreted by Saccharomyces cerevisiae, Pikt killer activity is not mediated by an increase in membrane permeability. Purification of the toxin yielded a homogeneous protein of about 8 kDa, which showed a marked similarity to ubiquitin in terms of molecular mass and N-terminal sequences. Pikt is also specifically recognized by anti-bovine ubiquitin antibodies and, similar to ubiquitin-like peptides, is not absorbed by DEAE-cellulose. However, Pikt differs from ubiquitin in its sensitivity to proteolytic enzymes. Therefore, Pikt appears to be a novel ubiquitin-like peptide that has killer activity.
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