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PLANT PHYSIOLOGY , Vol 110, Issue 3 957-964, Copyright © 1996 by American Society of Plant Biologists
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CELL BIOLOGY AND SIGNAL TRANSDUCTION |
Fusicoccin Binding to Its Plasma Membrane Receptor and the Activation of the Plasma Membrane H+-ATPase (III. Is There a Direct Interaction between the Fusicoccin Receptor and the Plasma Membrane H+-ATPase?)
M. I. De Michelis, F. Rasi-Caldogno, M. C. Pugliarello and C. Olivari
Istituto Botanico, Universita di Genova, corso Dogali 1/C, 16136 Genova, Italy (M.I.D.M.)
A radioimmunoassay using antibodies raised against bovine serum
albumin-conjugated fusicoccin (FC) was applied to measure FC bound to the
plasma membrane (PM) isolated from seedlings of radish (Raphanus sativus
L.) and of Arabidopsis thaliana treated in vivo plus or minus the toxin. FC
bound to the PM from seedlings treated with 5 [mu]M FC was 2-fold (radish)
to 7-fold (A. thaliana) higher than the binding capacity of control PM. FC
binding depended on the duration of the in vivo treatment but was
unaffected by cycloheximide. When FC binding and the PM H+-ATPase activity
were compared under different conditions (in vivo or in vitro treatment of
different lengths or with different concentrations of FC), a strict linear
relation between FC binding and the activation of the PM H+-ATPase was
observed in both plant materials under all the conditions tested.
Comparison between the maximum binding capacity and the amount of H+-ATPase
observed in PM from the two plant materials suggest a one-to-one
stoichiometry between the FC receptor and the PM H+-ATPase.
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