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Published online before print June 13, 2008, 10.1110/ps.035972.108
Protein Science (2008), 17:1522-1530. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
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The structure of "defective in induced resistance" protein of Arabidopsis thaliana, DIR1, reveals a new type of lipid transfer protein

Marie-Bernard Lascombe1, Bénédicte Bakan2, Nathalie Buhot3, Didier Marion2, Jean-Pierre Blein4, Valéry Larue1, Chris Lamb3, and Thierry Prangé1

1 Université Paris Descartes, Faculté de Pharmacie, CNRS, Laboratoire de Cristallographie et RMN Biologiques (UMR 8015), Paris 75006, France
2 Unité de Recherche Biopolymères Interactions Assemblages, Institut National de la Recherche Agronomique (INRA), 44316-Nantes Cedex, France
3 John Innes Centre, Norwich NR4 7UH, United Kingdom
4 Unité de Phytopharmacie et Biochimie des Interactions Cellulaires (UMR 692 CNRS INRA), Domaine d'Epoisses, BP 86510, 2110-Dijon Cedex, France

(RECEIVED April 24, 2008; FINAL REVISION June 13, 2008; ACCEPTED June 13, 2008)

Screening of transfer DNA (tDNA) tagged lines of Arabidopsis thaliana for mutants defective in systemic acquired resistance led to the characterization of dir1-1 (defective in induced resistance [systemic acquired resistance, SAR]) mutant. It has been suggested that the protein encoded by the dir1 gene, i.e., DIR1, is involved in the long distance signaling associated with SAR. DIR1 displays the cysteine signature of lipid transfer proteins, suggesting that the systemic signal could be lipid molecules. However, previous studies have shown that this signature is not sufficient to define a lipid transfer protein, i.e., a protein capable of binding lipids. In this context, the lipid binding properties and the structure of a DIR1–lipid complex were both determined by fluorescence and X-ray diffraction. DIR1 is able to bind with high affinity two monoacylated phospholipids (dissociation constant in the nanomolar range), mainly lysophosphatidyl cholines, side-by-side in a large internal tunnel. Although DIR1 shares some structural and lipid binding properties with plant LTP2, it displays some specific features that define DIR1 as a new type of plant lipid transfer protein. The signaling function associated with DIR1 may be related to a specific lipid transport that needs to be characterized and to an additional mechanism of recognition by a putative receptor, as the structure displays on the surface the characteristic PxxP structural motif reminiscent of SH3 domain signaling pathways.

Keywords: DIR1; Arabidopsis thaliana; systemic induced resistance; lipid transfer protein; SH3 signaling pathway; polyproline


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