Fatty acids bind to the fungal elicitor cryptogein and compete with sterols

FEBS Letters

Vauthrin, S.²  Maume, B.F.²  Prangé, T.⁵  Osman, H.²  Mikes, V.³  Blein, J.-P.²  Milat, M.-L.²  Ponchet, M.⁴  Marion, D.¹ 

[1] Laboratoire de Biochimie et Technologie des Protéines, INRA, BP 71627, 44316 Nantes Cedex 03, France;UMR 692 INRA, Université de Bourgogne, Laboratoire de Phytopharmacie et de Biochimie des Interactions Cellulaires, INRA, BP 86510, 21065 Dijon Cedex, France;Department of Biochemistry, Faculty of Science, Masaryk University, Kotlarska 2, 61137 Brno, Czech Republic;IPMSV, INRA, BP 2078, 06606 Antibes Cedex, France;LCRB, Faculté de Pharmacie, 4 av. de l'Observatoire, 75270 Paris Cedex 06, France

关键词: Elicitin;    Lipid–protein interaction;    Fatty acid;    Sterol;    Phytophthora;    DHE;    Δ5;    7;    9(11)22-ergostatetraen-3β-ol (dehydroergosterol);    FA;    fatty acid;    FABP;    fatty acid binding protein;    SCP;    sterol carrier protein;   

DOI  :  10.1016/S0014-5793(01)02078-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Cryptogein is a proteinaceous elicitor of plant defense reactions which also exhibits sterol carrier properties. In this study, we report that this protein binds fatty acids. The stoichiometry of the fatty acid–cryptogein complex is 1:1. Linoleic acid and dehydroergosterol compete for the same site, but elicitin affinity is 27 times lower for fatty acid than for sterol. We show that C7 to C12 saturated and C16 to C22 unsaturated fatty acids are the best ligands. The presence of double bonds markedly increases the affinity of cryptogein for fatty acids. A comparison between elicitins and known lipid transfer proteins is discussed.

【 授权许可】

Unknown