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THE STRUCTURE OF "DEFECTIVE IN INDUCED RESISTANCE" PROTEIN OF ARABIDOPSIS THALIANA, DIR1, REVEALS A NEW TYPE OF LIPID TRANSFER PROTEIN

¹ Universite Paris Descartes;
² INRA Nantes;
³ INRA Dijon;
⁴ John Innes Centre

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

Screening of transfer T-DNA tagged lines of A. thaliana for mutants defective in systemic acquired resistance, led to the characterization of dir1-1 (defective in induced resistance) 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: Lipoproteins; Protein Structure/Folding; Structure; Structure/function studies; Crystallography; Fluorescence; Hydrophobic interactions; Protein crystallization; Arabidopsis thaliana; systemic induced resistance; lipid transfer protein; SH3 signaling pathway; polyproline

⁵ E-mail: thierry.prange{at}univ-paris5.fr

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