A lipid transfer protein binds to a receptor involved in the control of plant defence responses

FEBS Letters

Maume, B.F.¹  Mikès, V.⁴  Tran, V.³  Blein, J.-P.¹  Buhot, N.¹  Milat, M.-L.¹  Kader, J.-C.⁷  Ponchet, M.²  Marion, D.⁵  Douliez, J.-P.⁵  Jacquemard, A.⁶ 

[1] UMR 692 INRA/Université de Bourgogne, Laboratoire de Phytopharmacie et de Biochimie des Interactions Cellulaires, INRA, P.O. Box 86510, 21065 Dijon Cedex, France;IPMSV, INRA, P.O. Box 2078, 06606 Antibes Cedex, France;Unité de Physico-chimie des Macromolécules, INRA, P.O. Box 71627, 44316 Nantes Cedex, 03, France;Department of Biochemistry, Faculty of Science, Masaryk University, Kotlarska 2, 61137 Brno, Czech Republic;Laboratoire de Biochimie et Technologie des Protéines, INRA, P.O. Box 71627, 44316 Nantes Cedex 03, France;UMR 5584 CNRS, Laboratoire de Topologie, Département de Mathématiques, Université de Bourgogne, P.O. Box 47870, 21078 Dijon Cedex, France;Laboratoire de Physiologie Cellulaire et Moléculaire CNRS/Université Pierre et Marie Curie, UMR7632, case 154, 4 place Jussieu, 75252 Paris Cedex 05, France

关键词: Allostery;    Elicitin;    Lipid transfer protein;    Receptor;   

DOI  :  10.1016/S0014-5793(01)03116-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Lipid transfer proteins (LTPs) and elicitins are both able to load and transfer lipidic molecules and share some structural and functional properties. While elicitins are known as elicitors of plant defence mechanisms, the biological function of LTP is still an enigma. We show that a wheat LTP1 binds with high affinity sites. Binding and in vivo competition experiments point out that these binding sites are common to LTP1 and elicitins and confirm that they are the biological receptors of elicitins. A mathematical analysis suggests that these receptors could be represented by an allosteric model corresponding to an oligomeric structure with four identical subunits.

【 授权许可】

Unknown