The H+‐ATPase purified from maize root plasma membranes retains fusicoccin in vivo activation

FEBS Letters

Fogliano, Vincenzo¹  Nasta, Daniela²  Fullone, Maria Rosaria³  Marra, Mauro²  Zambardi, Alessandra²  Aducci, Patrizia² 

[1] Dipartimento di Scienza degli Alimenti, Università di Napoli ‘Federico II’ Via Università 100, Portici, I-80055 Napoli, Italy;Dipartimento di Biologia, Università di Roma ‘Tor Vergata’ Via della Ricerca Scientifica, I-00133 Roma, Italy;Dipartimento di Scienze Biochimiche ‘A. Rossi Fanelli’ Università dr Roma ‘La Sapienza’, P.le A. Moro 5, I-00185 Roma, Italy

关键词: Signal transduction;    H+-ATPase;    14-3-3 protein;    Fusicoccin receptor;    FC;    fusicoccin;    [3H]FC;    tritiated dihydrofusicoccin;    ACMA;    9-amino-6-chloro-2-methoxyacridine;    BTP;    1;    3-bis[tris(hydroxymethyl)methylamino]propane;    DTT;    dithiothreitol;    MOPS;    3-(N-morpholino)propanesulfonic acid;    PMSF;    phenylmethylsulfonyl fluoride;    PC;    phosphatidylcholine;    PE;    phosphatidylethanolamine;    PVDF;    polyvinylidene difluoride;   

DOI  :  10.1016/0014-5793(96)00187-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown