Isolation of a novel auxin receptor from soluble fractions of rice (Oryza sativa L.) shoots

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.