A lipid transfer protein binds to a receptor involved in the control of plant defence responses.
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.
Buhot
N
N
UMR 692 INRA/Université de Bourgogne, Laboratoire de Phytopharmacie et de Biochemie des Interactions Cellulaires, Dijon, France.
Douliez
J P
JP
Jacquemard
A
A
Marion
D
D
Tran
V
V
Maume
B F
BF
Milat
M L
ML
Ponchet
M
M
Mikès
V
V
Kader
J C
JC
Blein
J P
JP
D020418:Algal Proteins / Q000737:chemistry / Q000378:metabolism; D000495:Allosteric Site; D052179:Antigens, Plant; D001665:Binding Sites; D001667:Binding, Competitive; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D004305:Dose-Response Relationship, Drug; D005656:Fungal Proteins; D008024:Ligands; D050356:Lipid Metabolism; D008958:Models, Molecular; D008962:Models, Theoretical; D010838:Phytophthora / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D013997:Time Factors; D014026:Nicotiana / Q000378:metabolism; D014908:Triticum / Q000737:chemistry
D020418:Algal Proteins; D052179:Antigens, Plant; D002352:Carrier Proteins; D005656:Fungal Proteins; D008024:Ligands; D010940:Plant Proteins; C061032:cryptogein protein, Phytophthora cryptogea; C511920:lipid transfer proteins, plant