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Grandmougin-Ferjani A, Schuler-Muller I, Hartmann MA. Sterol Modulation of the Plasma Membrane H+-ATPase Activity from Corn Roots Reconstituted into Soybean Lipids. Plant Physiol. 1997;113(1):163-174doi: 10.1104/pp.113.1.163.
Grandmougin-Ferjani, A., Schuler-Muller, I., & Hartmann, M. A. (1997). Sterol Modulation of the Plasma Membrane H+-ATPase Activity from Corn Roots Reconstituted into Soybean Lipids. Plant physiology, 113(1), 163-174. https://doi.org/10.1104/pp.113.1.163
Grandmougin-Ferjani, A., et al. "Sterol Modulation of the Plasma Membrane H+-ATPase Activity from Corn Roots Reconstituted into Soybean Lipids." Plant physiology vol. 113,1 (1997): 163-174. doi: https://doi.org/10.1104/pp.113.1.163
Grandmougin-Ferjani A, Schuler-Muller I, Hartmann MA. Sterol Modulation of the Plasma Membrane H+-ATPase Activity from Corn Roots Reconstituted into Soybean Lipids. Plant Physiol. 1997 Jan;113(1):163-174. doi: 10.1104/pp.113.1.163. PMID: 12223599; PMCID: PMC158127.
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Plant Physiol. 1997 Jan;113(1):163-174. doi: 10.1104/pp.113.1.163.

Sterol Modulation of the Plasma Membrane H+-ATPase Activity from Corn Roots Reconstituted into Soybean Lipids.

Plant physiology

A. Grandmougin-Ferjani, I. Schuler-Muller, M. A. Hartmann

Affiliations

  1. Institut de Biologie Moleculaire des Plantes, du Centre National de la Recherche Scientifique, 28 rue Goethe, 67083 Strasbourg Cedex, France.

PMID: 12223599 PMCID: PMC158127 DOI: 10.1104/pp.113.1.163

Abstract

A partially purified H+-ATPase from the plasma membrane (PM) of corn (Zea mays L.) roots was inserted into vesicles prepared with soybean (Glycine max L.) phospholipids and various concentrations of individual sterols using either a freeze-thaw sonication or an octylglucoside dilution procedure. Both methods yielded a functional enzyme that retained its native characteristics. We have investigated the effects of typical plant sterols (i.e. sitosterol, stigmasterol, and 24-methylcholesterol) on both ATP hydrolysis and H+ pumping by the reconstituted corn root PM ATPase. We have also checked the influence of cholesterol and of two unusual sterols, 24-methylpollinastanol and 14[alpha],24-dimethylcholest-8-en-3[beta]-ol. Here we present evidence for a sterol modulation of the plant PM H+-ATPase activity. In particular, cholesterol and stigmasterol were found to stimulate the pump, especially when present at 5 mol%, whereas all of the other sterols tested behaved as inhibitors at any concentration in proteoliposomes. In all situations H+ pumping was shown to be more sensitive to a sterol environment than was ATP hydrolysis. Our results suggest the occurrence of binding sites for sterols on the plant PM H+-ATPase.

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