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Vol. 15, Issue 11, 5047-5052, November 2004
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* Laboratoire de Phytopharmacie, Institut National de la Recherche Agronomique-Université de Bourgogne-Etablissement National Enseignement Supérieur Agronomique de Dijon, Unité Mixte de Recherches 692, BP 86510, Dijon-Cedex 21065, France;
Laboratoire de Physiologie, Biochimie et Biologie Moléculaire Végétales, Université de Poitiers-Centre National de la Recherche Scientifique, Unité Mixte de Recherches 6161, Bâtiment de Botanique, Poitiers-Cedex 86022, France;
¶ Unité Mixte de Recherches, Interactions Plantes-Microorganismes et Santé Végétale, Institut National de la Recherche Agronomique, BP 167, Sophia Antipolis Cedex 06903, France; and
# Unité de Recherche sur les Protéines Végétales et leurs Interactions, Institut National de la Recherche Agronomique, 44316, Nantes Cedex 3, France
Submitted July 9, 2004;
Accepted August 16, 2004
Monitoring Editor: Guido Guidotti
Plant lipid transfer proteins (LTPs) are small, cysteine-rich proteins secreted into the extracellular space. They belong to the pathogenesis-related proteins (PR-14) family and are believed to be involved in several physiological processes including plant disease resistance, although their precise biological function is still unknown. Here, we show that a recombinant tobacco LTP1 is able to load fatty acids and jasmonic acid. This LTP1 binds to specific plasma membrane sites, previously characterized as elicitin receptors, and is shown to be involved in the activation of plant defense. The biological properties of this LTP1 were compared with those of LTP1-linolenic and LTP1-jasmonic acid complexes. The binding curve of the LTP1-linolenic acid complex to purified tobacco plasma membranes is comparable to the curve obtained with LTP1. In contrast, the LTP1-jasmonic acid complex shows a strongly increased interaction with the plasma membrane receptors. Treatment of tobacco plants with LTP1-jasmonic acid resulted in an enhancement of resistance toward Phytophthora parasitica. These effects were absent upon treatment with LTP1 or jasmonic acid alone. This work presents the first evidence for a biological activity of a LTP1 and points out the crucial role of protein-specific lipophilic ligand interaction in the modulation of the protein activity.
Abbreviations used: FA, fatty acid; JA, jasmonic acid; LA, linolenic acid; LTP, lipid transfer protein, SAR, systemic acquired resistance; TFA, trifluoroacetic acid, TNS, 2-p-toluidinonaphtalene-6-sulfonate.
These authors contributed equally to this work.
Present address: John Innes Centre, Norwich Research Park, Norwich NR4 7UH, UK.
|| Corresponding author. E-mail address: eric.gomes{at}univpoitiers.fr.
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