ATP-driven potassium transport in right-side-out membrane vesicles via the Kdp system of Escherichia coli

Biochim Biophys Acta. 1993 Jun 10;1143(1):62-6. doi: 10.1016/0005-2728(93)90216-3.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / antagonists & inhibitors
  • Adenosine Triphosphatases / metabolism*
  • Adenosine Triphosphate / biosynthesis*
  • Anti-Bacterial Agents / metabolism
  • Biological Transport, Active
  • Cation Transport Proteins*
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins*
  • Liposomes
  • Macrolides*
  • Membrane Proteins / metabolism
  • Phosphoenolpyruvate / metabolism
  • Potassium / metabolism*
  • Proline / metabolism
  • Time Factors
  • Vanadates / pharmacology

Substances

  • Anti-Bacterial Agents
  • Cation Transport Proteins
  • Escherichia coli Proteins
  • Liposomes
  • Macrolides
  • Membrane Proteins
  • Vanadates
  • Phosphoenolpyruvate
  • bafilomycin B1
  • Adenosine Triphosphate
  • Proline
  • Adenosine Triphosphatases
  • potassium translocating Kdp-ATPase, E coli
  • Potassium