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Applied and Environmental Microbiology, February 2009, p. 1129-1134, Vol. 75, No. 4
0099-2240/09/$08.00+0 doi:10.1128/AEM.01837-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Istituto di Biotecnologie Biochimiche, Università Politecnica delle Marche, Via Ranieri, 60131 Ancona, Italy,1 Dipartimento SAIFET sez di Microbiologia Alimentare, Industriale e Ambientale, Università Politecnica delle Marche, Via Brecce Bianche, 60131 Ancona, Italy,2 Dipartimento di Scienze Ambientali Agrarie e Biotecnologie Agroalimentari, Università degli Studi di Sassari, Viale Italia 39, 07100 Sassari, Italy3
Received 8 August 2008/ Accepted 16 December 2008
The yeast strain Pichia anomala DBVPG 3003 secretes a killer toxin (Pikt) that has antifungal activity against Brettanomyces/Dekkera sp. yeasts. Pikt interacts with β-1,6-glucan, consistent with binding to the cell wall of sensitive targets. In contrast to that of 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.
Published ahead of print on 29 December 2008.
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