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Fusicoccin Binding to Its Plasma Membrane Receptor and the Activation of the Plasma Membrane H+-ATPase1
IV. Fusicoccin Induces the Association between the Plasma Membrane H+-ATPase and the Fusicoccin Receptor

Claudio Olivari*, Cristina Meanti, Maria Ida De Michelis, and Franca Rasi-Caldogno2

Dipartimento di Biologia, Università di Milano, via G. Celoria 26, 20133 Milano, Italy (C.O., C.M., F.R.-C.); and Istituto di Botanica, Università di Genova, corso Dogali 1c, 16136 Genova, Italy (M.I.D.M.)

Different approaches were utilized to investigate the mechanism by which fusicoccin (FC) induces the activation of the H+-ATPase in plasma membrane (PM) isolated from radish (Raphanus sativus L.) seedlings treated in vivo with (FC-PM) or without (C-PM) FC. Treatment of FC-PM with different detergents indicated that PM H+-ATPase and the FC-FC-binding-protein (FCBP) complex were solubilized to a similar extent. Fractionation of solubilized FC-PM proteins by a linear sucrose-density gradient showed that the two proteins comigrated and that PM H+-ATPase retained the activated state induced by FC. Solubilized PM proteins were also fractionated by a fast-protein liquid chromatography anion-exchange column. Comparison between C-PM and FC-PM indicated that in vivo treatment of the seedlings with FC caused different elution profiles; PM H+-ATPase from FC-PM was only partially separated from the FC-FCBP complex and eluted at a higher NaCl concentration than did PM H+-ATPase from C-PM. Western analysis of fast-protein liquid chromatography fractions probed with an anti-N terminus PM H+-ATPase antiserum and with an anti-14-3-3 antiserum indicated an FC-induced association of FCBP with the PM H+-ATPase. Analysis of the activation state of PM H+-ATPase in fractions in which the enzyme was partially separated from FCBP suggested that the establishment of an association between the two proteins was necessary to maintain the FC-induced activation of the enzyme.

1   This work was supported by Ministero per le Risorse Agricole, Alimentari e Forestali in the frame of the Piano Nazionale per le Biotecnologie Vegetali and by Consiglio Nazionale delle Ricerche, coordinated project Membrane, Apoplasto e Omeostasi Cellulare.
2   Franca Rasi-Caldogno, who played a pivotal role in this work, died prematurely before its completion.
*   Corresponding author; e-mail fimca{at}imiucca.csi.unimi.it; fax 39-2-26-60-4399.

Plant Physiol. (1998) 116: 529-537
Copyright Clearance Center:   0032-0889/98/116/0529/09
© 1998 American Society of Plant Physiologists




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