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Plant Biol (Stuttg) 2003; 5(2): 116-124
DOI: 10.1055/s-2003-40723
Review Article

Georg Thieme Verlag Stuttgart · New York

The Comparative Analysis of Osmotins and Osmotin-Like PR-5 Proteins

S. Anžlovar 1 , M. Dermastia 1
  • 1University of Ljubljana, Biotechnical Faculty, Department of Biology, Večna pot 111, 1000 Ljubljana, Slovenia
Further Information

Publication History

Publication Date:
21 July 2003 (online)

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Abstract

One of the ways that plants respond to biotic and/or abiotic stress factors is the accumulation of pathogenesis-related proteins of class 5 (PR-5), which are evolutionary conserved in the plant kingdom. Within the PR-5 family, a distinct subgroup of osmotin and closely related proteins has been characterized. In contrast to the extracellular forms of PR-5 proteins, osmotins presumably accumulate in the vacuole of the cell. They contain a C-terminal propeptide that is considered to be a determinant for vacuolar targeting. The comparison of the three-dimensional structure of tobacco PR-5 d with the sequences of some osmotins showed that the proteins consist of three conserved domains, with the acidic cleft between domains I and II. Besides the constitutive species and tissue-specific presence, the osmotins are also induced by several abiotic and biotic stresses. Among them, fungal infections can elicit osmotin gene expression, and most known proteins from the family have antifungal activity in in vitro assays. In agreement with the osmotin structure and data on the activity of similar proteins, a two-step mechanism, which involves reaction of osmotins with the fungal wall and the permeabilization of fungal membranes, is discussed.

Key words

PR-5 - structure - gene expression - mechanism of antifungal activity

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M. Dermastia

Department of Biology, Biotechnical Faculty
University of Ljubljana

Večna pot 111

1000 Ljubljana

Slovenia

Email: marina.dermastia@uni-lj.si;

Section Editor: L. A. C. J. Voesenek