6533b82efe1ef96bd12927c6
RESEARCH PRODUCT
Functional reconstitution of a proton-translocating system responsive to fusicoccin
Jean-pierre BleinMichel RossignolMaria Rosaria FullonePatrizia AducciAlessandro BallioRené Scallasubject
0106 biological sciencesATPase[SDV]Life Sciences [q-bio]01 natural sciences03 medical and health scienceschemistry.chemical_compoundProton transportGlycosidesBinding siteComputingMilieux_MISCELLANEOUSFluorescent Dyes030304 developmental biologychemistry.chemical_classification0303 health sciencesLiposomeBinding SitesMultidisciplinarybiologyAminoacridinesCell MembraneBiological activityPlants[SDV] Life Sciences [q-bio]Proton-Translocating ATPasesMembraneEnzymeSolubilitychemistryBiochemistryFusicoccinLiposomesbiology.proteinResearch Article010606 plant biology & botanydescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1988-11-01 |