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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1988 Nov;85(21):7849–7851. doi: 10.1073/pnas.85.21.7849

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

P Aducci 1, A Ballio 1, J P Blein 1, M R Fullone 1, M Rossignol 1, R Scalla 1
PMCID: PMC282294  PMID: 2903497

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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