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Fusicoccin Binding to Its Plasma Membrane Receptor and the Activation of the Plasma Membrane H⁺-ATPase: 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-Caldogno
Plant Physiology
Vol. 116, No. 2 (Feb., 1998), pp. 529-537
Stable URL: http://www.jstor.org/stable/4278123
Page Count: 9
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Fusicoccin Binding to Its Plasma Membrane Receptor and the Activation of the Plasma Membrane H⁺-ATPase: IV. Fusicoccin Induces the Association between the Plasma Membrane H⁺-ATPase and the Fusicoccin Receptor
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Abstract

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.

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