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THE PLANT CELL, Vol 9, Issue 10 1805-1814, Copyright © 1997 by American Society of Plant Biologists
The 14-3-3 Protein Interacts Directly with the C-Terminal Region of the Plant Plasma Membrane H+-ATPase
T. Jahn, A. T. Fuglsang, A. Olsson, I. M. Bruntrup, D. B. Collinge, D. Volkmann, M. Sommarin, M. G. Palmgren and C. Larsson
Department of Plant Biochemistry, Lund University, P.O. Box 117, S-22100 Lund, Sweden
Accumulating evidence suggests that 14-3-3 proteins are involved in the
regulation of plant plasma membrane H+-ATPase activity. However, it is not
known whether the 14-3-3 protein interacts directly or indirectly with the
H+-ATPase. In this study, detergent-solubilized plasma membrane H+-ATPase
isolated from fusicoccin-treated maize shoots was copurified with the
14-3-3 protein (as determined by protein gel blotting), and the H+-ATPase
was recovered in an activated state. In the absence of fusicoccin
treatment, H +-ATPase and the 14-3-3 protein were well separated, and the
H+-ATPase was recovered in a nonactivated form. Trypsin treatment removed
the 10-kD C-terminal region from the H+-ATPase as well as the 14-3-3
protein. Using the yeast two-hybrid system, we could show a direct
interaction between Arabidopsis 14-3-3 GF14-0 and the last 98 C-terminal
amino acids of the Arabidopsis AHA2 plasma membrane H+-ATPase. We propose
that the 14-3-3 protein is a natural ligand of the plasma membrane
H+-ATPase, regulating proton pumping by displacing the C-terminal
autoinhibitory domain of the H+-ATPase.
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