ATP-driven potassium transport in right-side-out membrane vesicles via the Kdp system of Escherichia coli.
The ATP-generating system described by Hugenholtz, J., Hong, J.-S. and Kaback, H.R. ((1981) Proc. Natl. Acad. Sci. USA 78, 3446-3449) has been used to synthesize ATP up to 1.8 mM in right-side-out membrane vesicles from Escherichia coli. This ATP level was sufficient to drive uptake of potassium ions via the Kdp-ATPase. In the kdp wild type strain about 110 nmoles K+/mg membrane protein were accumulated. This process was still partially sensitive to the well-known inhibitors of P-type ATPases, orthovanadate and bafilomycin B1.
Universität Osnabrück, Fachbereich Biologie/Chemie, Arbeitsgruppe Mikrobiologie, Osnabrück, Germany.
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Altendorf
D000251:Adenosine Triphosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000096:biosynthesis*; D000900:Anti-Bacterial Agents / Q000378:metabolism; D001693:Biological Transport, Active; D027682:Cation Transport Proteins; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D008081:Liposomes; D018942:Macrolides; D008565:Membrane Proteins / Q000378:metabolism; D010728:Phosphoenolpyruvate / Q000378:metabolism; D011188:Potassium / Q000378:metabolism*; D011392:Proline / Q000378:metabolism; D013997:Time Factors; D014638:Vanadates / Q000494:pharmacology
D000900:Anti-Bacterial Agents; D027682:Cation Transport Proteins; D029968:Escherichia coli Proteins; D008081:Liposomes; D018942:Macrolides; D008565:Membrane Proteins; D014638:Vanadates; D010728:Phosphoenolpyruvate; C052501:bafilomycin B1; D000255:Adenosine Triphosphate; D011392:Proline; D000251:Adenosine Triphosphatases; C058166:potassium translocating Kdp-ATPase, E coli; D011188:Potassium