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Plant and Cell Physiology 2004 45(11):1669-1680; doi:10.1093/pcp/pch189
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© 2004 Oxford University Press

Pn-AMP1, a Plant Defense Protein, Induces Actin Depolarization in Yeasts

Ja Choon Koo1,2,4, Boyoung Lee1,4, Michael E. Young3,4, Sung Chul Koo1, John A. Cooper3, Dongwon Baek1, Chae Oh Lim1, Sang Yeol Lee1, Dae-Jin Yun1,5 and Moo Je Cho1

1 Division of Applied Life Science (BK21 program), PMBBRC, and Environmental Biotechnology National Core Research Center, Graduate School of Gyeongsang National University, Jinju 660-701, Korea
2 Division of Molecular Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Korea
3 Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110, U.S.A.

Pn-AMP1, Pharbitis nil antimicrobial peptide 1, is a small cysteine-rich peptide implicated in host-plant defense. We show here that Pn-AMP1 causes depolarization of the actin cytoskeleton in Saccharomyces cerevisiae and Candida albicans. Pn-AMP1 induces rapid depolarization of actin cables and patches within 15 min. Increased osmolarity or temperature induces transient actin depolarization and results in increased sensitivity to Pn-AMP1, while cells conditioned to these stresses show less sensitivity. Mutations in components of a cell wall integrity pathway (Wsc1p, Rom2p, Bck1p and Mpk1p), which regulate actin repolarization, result in increased sensitivity to Pn-AMP1. A genetic screen reveals that mutations in components of the {alpha}-1,6-mannosyltransferase complex (Mnn10p, Mnn11p and Och1p), which regulate mannosylation of cell wall proteins, confer resistance to Pn-AMP1. FITC-conjugated Pn-AMP1 localizes to the outer surface of the cell with no significant staining observed in spheroplasts. Taken together, these results indicate that cell wall proteins are determinants of resistance to Pn-AMP1, and the ability of a plant defense protein to induce actin depolarization is important for its antifungal activity.

4 The first three authors contributed equally to this work.

5 Corresponding author: E-mail, djyun{at}nongae.gsnu.ac.kr; Fax, +82-55-759-9363.


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