Relationship of the Escherichia coli TrkA system of potassium ion uptake with the F0F1-ATPase under growth conditions without anaerobic or aerobic respiration.
K+ uptake by the Escherichia coli TrkA system is unusual in that it requires both ATP and deltamuH+; a relation with H+ circulation through the membrane is therefore suggested. The relationship of this system with the F0F1-ATPase was studied in intact cells grown under different conditions. A significant increase of the N,N'-dicyclohexylcarbodiimide(DCCD)-inhibited H+ efflux through the F0F1 by 5 mM K+, but not by Na+ added into the potassium-free medium was revealed only in fermenting wild-type or parent cells, that were grown under anaerobic conditions without anaerobic or aerobic respiration and with the production of H2. Such an increase disappeared in the deltaunc or the trkA mutants that have altered F0F1 or defective TrkA, respectively. This finding indicates a closed relationship between TrkA and F0F1, with these transport systems being associated in a single mechanism that functions as an ATP-driven H(+)-K(+)-exchanging pump. A DCCD-inhibited H(+)-L(+)-exchange through these systems with the fixed stoichiometry of H+ and K+ fluxes (2H+/K+) and a higher K+ gradient between the cytoplasm and the external medium were also found in these bacteria. They were not observed in cells cultured under anaerobic conditions in the presence of nitrate or under aerobic conditions with respiration and without production of H2. The role of anaerobic or aerobic respiration as a determinant of the relationship of the TrkA with the F0F1 is postulated. Moreover, an increase of DCCD-inhibited H+ efflux by added K+, as well as the characteristics of DCCD-sensitive H(+)-K(+)-exchange found in a parent strain, were lost in the arcA mutant with a defective Arc system, suggesting a repression of enzymes in respiratory pathways. In addition, K+ influx in the latest mutant was not markedly changed by valinomycin or with temperature. The arcA gene product or the Arc system is proposed to be implicated in the regulation of the relationship between TrkA and F0F1.
Trchounian
A
A
Department of Biophysics, Biological Faculty of the Yerevan State University, Armenia.
Ohanjanyan
Y
Y
Bagramyan
K
K
Vardanian
V
V
Zakharyan
E
E
Vassilian
A
A
Davtian
M
M
D000332:Aerobiosis; D000693:Anaerobiosis; D051777:AraC Transcription Factor; D001426:Bacterial Proteins / Q000378:metabolism*; D002352:Carrier Proteins / Q000378:metabolism*; D004024:Dicyclohexylcarbodiimide / Q000494:pharmacology; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D029968:Escherichia coli Proteins; D005285:Fermentation; D017136:Ion Transport / Q000187:drug effects; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism*; D009154:Mutation; D010100:Oxygen / Q000378:metabolism*; D011188:Potassium / Q000378:metabolism*; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D020917:Receptor, trkA; D012097:Repressor Proteins / Q000235:genetics / Q000378:metabolism; D014157:Transcription Factors
D051777:AraC Transcription Factor; C497371:AraC protein, E coli; D001426:Bacterial Proteins; D002352:Carrier Proteins; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; D004024:Dicyclohexylcarbodiimide; D020917:Receptor, trkA; D006180:Proton-Translocating ATPases; D011188:Potassium; D010100:Oxygen