title: Isolation of a novel auxin receptor from soluble fractions of rice (Oryza sativa L.) shoots.
abstract: An auxin binding protein (ABP) was isolated from the shoots of rice seedlings and characterized. The ABP was found to be a monomer with a molecular mass of 57 kDa and play a crucial role via auxin binding in regulating H+ translocation activity of the plasma membrane in a typical biphasic manner. The results of binding equilibrium experiments indicate that the ABP binds indole 3-acetic acid with a high affinity (Kd = 1.9 x 10(-8) M), having four primary binding sites for auxin and some secondary sites with low auxin affinities. The ABP appears to have an unambiguous auxin receptor function.
authors.affiliation: Department of Agricultural Chemistry, College of Agriculture and Life Sciences, Seoul National University, Suwon, South Korea.
authors.forename: Y S
authors.initials: YS
authors.lastname: Kim
authors.forename: D
authors.initials: D
authors.lastname: Kim
authors.forename: J
authors.initials: J
authors.lastname: Jung
mesh_terms: D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism; D007210:Indoleacetic Acids / Q000378:metabolism*; D007700:Kinetics; D012275:Oryza / Q000378:metabolism*; D010937:Plant Growth Regulators; D010940:Plant Proteins; D018520:Plant Shoots; D006180:Proton-Translocating ATPases / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*
chemical_list: D007210:Indoleacetic Acids; D010937:Plant Growth Regulators; D010940:Plant Proteins; D011956:Receptors, Cell Surface; C046131:auxin receptor, plant; C030737:indoleacetic acid; D006180:Proton-Translocating ATPases