Relationship between the F0F1-ATPase and the K(+)-transport system within the membrane of anaerobically grown Escherichia coli. N,N'-dicyclohexylcarbodiimide-sensitive ATPase activity in mutants with defects in K(+)-transport.

A considerable (2-fold) stimulation of the DCCD-sensitive ATPase activity by K+ or Rb+, but not by Na+, over the range of zero to 100 mM was shown in the isolated membranes of E. coli grown anaerobically in the presence of glucose. This effect was observed only in parent and in the trkG, but not in the trkA, trkE, or trkH mutants. The trkG or the trkH mutant with an unc deletion had a residual ATPase activity not sensitive to DCCD. A stimulation of the DCCD-sensitive ATPase activity by K+ was absent in the membranes from bacteria grown anaerobically in the presence of sodium nitrate. Growth of the trkG, but not of other trk mutants, in the medium with moderate K+ activity did not depend on K+ concentration. Under upshock, K+ accumulation was essentially higher in the trkG mutant than in the other trk mutant. The K(+)-stimulated DCCD-sensitive ATPase activity in the membranes isolated from anaerobically grown E. coli has been shown to depend absolutely on both the F0F1 and the Trk system and can be explained by a direct interaction between these transport systems within the membrane of anaerobically grown bacteria with the formation of a single supercomplex functioning as a H(+)-K+ pump. The trkG gene is most probably not functional in anaerobically grown bacteria.