Cation transport mechanisms in Mycoplasma mycoides var. Capri cells. The nature of the link between K+ and Na+ transport

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Abstract
We have studied the links between the mechanisms of Na+, K+ and H+ movements in glycolysing Mycoplasma mycoides var. Capri cells. In the light of the results reported in the preceding paper [Benyoucef, Rigaud & Leblanc (1982) Biochem. J. 208, 529–538], we investigated certain properties of the membrane-bound ATPase of Mycoplasma cells, with special reference to its ionic requirements and sensitivity to specific inhibitors. Our findings show, first, that, although Na+ stimulated ATPase activity, K+ did not affect it, and, secondly, that NN′-dicyclocarboidi-imide and 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole (NBD) were potent inhibitors of the basal ATPase activity, which was unaffected by vanadate and ouabain. We also investigated the movements of Na+ and H+ under the experimental conditions applied to the study of the K+ uptake reported in the preceding paper, and found that when ‘Na+-loaded cells’ previously equilibrated with 22Na+ were diluted in a sodium-free medium, addition of glucose induced a rapid efflux of 22Na+. This energy-dependent efflux was independent of the presence of KCl in the medium. Studies of the changes in internal pH by 9-aminoacridine fluorescence or [14C]methylamine distribution indicated that the movement of Na+ was coupled to that of protons moving in the opposite direction, a finding that supports the presence of an Na+/H+ antiport. When Na+-loaded cells are diluted in an Na+-rich medium the Na+/H+ antiport is still active, but cannot decrease the intracellular Na+ concentration. Under such conditions, net 22Na+ extrusion is specifically dependent on the presence of K+ in the medium. The present results and those derived from the study of K+ accumulation (the preceding paper) can be rationalized by assuming that Mycoplasma mycoides var. Capri cells contain two transport systems for Na+ extrusion: an Na+/H+ antiport and an ATP-consuming Na+/K+-exchange system.

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