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A lipid transfer protein binds to a receptor involved in the control of plant defence responses
Author(s) -
Buhot N.,
Douliez J.-P.,
Jacquemard A.,
Marion D.,
Tran V.,
Maume B.F.,
Milat M.-L.,
Ponchet M.,
Mikès V.,
Kader J.-C.,
Blein J.-P.
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03116-7
Subject(s) - plant lipid transfer proteins , allosteric regulation , receptor , biochemistry , chemistry , binding site , microbiology and biotechnology , biology , biophysics , gene
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.