Purification and Properties of the F1Fo ATPase of Ilyobacter tartaricus, a Sodium Ion Pump

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Vol. 180, Issue 13, 3312-3316, July 1, 1998

Purification and Properties of the F₁F_o ATPase of Ilyobacter tartaricus, a Sodium Ion Pump

Sandra Neumann, Ulrich Matthey, Georg Kaim, and Peter Dimroth

Mikrobiologisches Institut, Eidgenössische Technische Hochschule Zürich, CH-8092 Zürich, Switzerland

The ATPase of Ilyobacter tartaricus was solubilized from the bacterial membranes and purified. Sodium dodecyl sulfate-polyacrylamidegel electrophoresis of the purified enzyme revealed the usualsubunit pattern of a bacterial F₁F_o ATPase. The polypeptides withapparent molecular masses of 56, 52, 35, 16.5, and 6.5 kDa wereidentified as the $alpha$ , $beta$ , $gamma$ , $varepsilon$ , and c subunits, respectively, byN-terminal protein sequencing and comparison with the sequencesof the corresponding subunits from the Na⁺-translocating ATPase of Propionigenium modestum. Two overlappingsequences were obtained for the polypeptides moving with an apparentmolecular mass of 22 kDa (tentatively assigned as b and $delta$ subunits).No sequence could be determined for the putative a subunit (apparentmolecular mass, 25 kDa). The c subunits formed a strong aggregatewith the apparent molecular mass of 50 kDa which required treatmentwith trichloroacetic acid for dissociation. The ATPase was inhibitedby dicyclohexyl carbodiimide, and Na⁺ ions protected the enzyme from this inhibition. The ATPase wasspecifically activated by Na⁺ or Li⁺ ions, markedly at high pH. After reconstitution into proteoliposomes,the enzyme catalyzed the ATP-dependent transport of Na⁺, Li⁺, or H⁺. Proton transport was specifically inhibited by Na⁺ or Li⁺ ions, indicating a competition between these alkali ions andprotons for binding and translocation across the membrane. Theseexperiments characterize the I. tartaricus ATPase as a new memberof the family of FS-ATPases, which use Na⁺ as the physiological coupling ion for ATP synthesis.

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