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The H + ‐ATPase purified from maize root plasma membranes retains fusicoccin in vivo activation
Author(s) -
Marra Mauro,
Fogliano Vincenzo,
Zambardi Alessandra,
Fullone Maria Rosaria,
Nasta Daniela,
Aducci Patrizia
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00187-1
Subject(s) - fusicoccin , atpase , enzyme , biochemistry , in vivo , chemistry , receptor , membrane , biophysics , biology , microbiology and biotechnology
The activity of ‘P‐type’ ATPases is modulated through the C‐terminal autoinhibitory domain. The molecular bases of this regulation are unknown. Their understanding demands functional and structural studies on the activated purified enzyme. In this paper the plasma membrane H + ‐ATPase from maize roots activated in vivo by fusicoccin was solubilised and fractionated by anion‐exchange HPLC. Results showed that the H + ‐ATPase separated from fusicoccin receptors retained fusicoccin activation and that it was more evident after enzyme insertion into liposomes. These data suggest that fusicoccin stimulation does not depend on a direct action of the fusicoccin receptor on the H + ‐ATPase, but rather, fusicoccin brings about a permanent modification of the H + ‐ATPase which very likely represents a general regulatory mechanism for ‘P‐type’ ATPases.