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The nature of the link between potassium transport and phosphate transport in Escherichia coli.

ABSTRACT: A series of mutants of Escherichia coli, combining defects in either of the two phosphate transport systems with defects in one or more of the potassium transport systems, was used to study the nature of the previously observed obligatory requirement for each one of these ions in the transport of the other. The results show that no pair of systems is obligatorily linked, and that either ion can be transported by any one of its systems, provided that a means of entry for the other ion is available. Furthermore, in the total absence of Pi, K+ entry accompanies the transport of other anions, such as aspartate, glutamate, sn-glycero-3-phosphate and glucose 6-phosphate. The results indicate that Pi and the other anions enter by symport with protons, and that a simultaneous K+/H+ exchange, which would serve to maintain the intracellular pH, is responsible for the observed K+ 'symport' with these anions.

SUBMITTER: Russell LM

PROVIDER: S-EPMC1161953 | biostudies-other | 1980 Jun

REPOSITORIES: biostudies-other

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Project description: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 (22)Na(+) were diluted in a sodium-free medium, addition of glucose induced a rapid efflux of (22)Na(+). 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 [(14)C]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 (22)Na(+) 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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The nature of the link between potassium transport and phosphate transport in Escherichia coli.

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