C. Oecking et K. Hagemann, Association of 14-3-3 proteins with the C-terminal antoinhibitory domain of the plant plasma-membrane H+-ATPase generates a fusicoccin-binding complex, PLANTA, 207(3), 1999, pp. 480-482
The plant plasma-membrane H+-ATPase (EC 3.6.1.35) contains a C-terminal aut
oinhibitory domain whose displacement from the catalytic site is caused by
treatment of intact plant tissue with the phytotoxin fusicoccin (FC). The F
C-induced activation of the H+-ATPase was proposed to involve a direct inte
raction of 14-3-3 proteins with the H+-ATPase. By analysing plasma membrane
s derived from leaves of Commelina communis L., direct biochemical evidence
has now been obtained for a complex between the C-terminus of the H+-ATPas
e and a 14-3-3 dimer. Stabilization of this complex was achieved by FC trea
tment in vivo or in vitro. Furthermore, the C-terminal domain of the H+-ATP
ase in association with a 14-3-3 dimer is essential for the creation of a f
unctional FC-binding complex.