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Functional reconstitution of a proton-translocating system responsive to fusicoccin.

By P Aducci, A Ballio, J P Blein, M R Fullone, M Rossignol and R Scalla

Abstract

Crude fusicoccin binding proteins and a partially purified plasma membrane H+-transporting ATPase (EC 3.6.1.34), both solubilized from maize tissues, were simultaneously inserted into liposomes by the freeze-thaw method. ATP-driven intravesicular acidification in the proteoliposomes, measured by the fluorescence quenching of the dye 9-amino-6-chloro-2-methoxyacridine, markedly increased upon addition of fusicoccin to the reconstituted system. This effect could not be observed when binding sites and ATPase preparations were separately reconstituted into the proteoliposomes, thus demonstrating that fusicoccin binding to its receptor is a prerequisite for ATPase stimulation

Topics: Research Article
Year: 1988
OAI identifier: oai:pubmedcentral.nih.gov:282294
Provided by: PubMed Central
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