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Leblanc, Nathalie; David, Karine; Grosclaude, Jeanne; Pradier, Jean-Marc; Barbier-Brygoo, Hélène; Labiau, Suzanne; Perrot-Rechenmann, Catherine
Journal of biological chemistry/The Journal of biological chemistry, 10/1999, Volume: 274, Issue: 40Journal Article
Interactions of a collection of monoclonal antibodies (mAbs) to the recombinant Nicotiana tabacumauxin-binding protein 1 (Nt-abp1) were extensively characterized using surface plasmon resonance. Dynamic interaction studies using combinations of Nt-abp1, synthetic peptides corresponding to conserved sequences within auxin-binding proteins, and the mAbs have shown that a number of the mAbs recognized discontinuous epitopes revealing the junction of distinct domains in the folded protein. In particular, the two putative auxin binding domains and the C terminus of the protein were shown to interact with each other in the folded protein. Using the auxin-induced electrical response of tobacco protoplasts as a functional assay, all the mAbs exhibited either auxin antagonist or hormonomimetic properties. These effects, measured for the first time in homologous conditions, confirm that Nt-abp1 is present at the plasma membrane and is involved in the activation of the auxin-dependent electrical response of tobacco protoplasts. Based on our surface plasmon resonance data, we propose that the key event leading to the activation of this auxin electrical response consists of a conformational change in Nt-abp1.
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