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ATP is required for K+ active transport in the archaebacterium Haloferax volcanii


The Archaebacterium Haloferax volcanii concentrates K+ up to 3.6 M. This creates a very large K+ ion gradient of between 500- to 1,000-fold across the cell membrane. H. volcanii cells can be partially depleted of their internal K+ but the residual K+ concentration cannot be lowered below 1.5 M. In these conditions, the cells retain the ability to take up potassium from the medium and to restore a high internal K+ concentration (3 to 3.2 M) via an energy dependent, active transport mechanism with a K m of between 1 to 2 mM. The driving force for K+ transport has been explored. Internal K+ concentration is not in equilibrium with ΔΨm suggesting that K+ transport cannot be accounted for by a passive uniport process. A requirement for ATP has been found. Indeed, the depletion of the ATP pool by arsenate or the inhibition of ATP synthesis by N,N′-dicyclohexylcarbodiimide inhibits by 100% K+ transport even though membrane potential ΔΨm is maintained under these conditions. By contrast, the necessity of a ΔΨm for K+ accumulation has not yet been clearly demonstrated. K+ transport in H. volcanii can be compared with K+ transport via the Trk system in Escherichia coli.

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Carbonylcyanide m-chlorophenyl-hydrazone




2-[N-morpholino] ethane sulfonic acid


3-[N-morpholino] propane sulfonic acid


Tris (hydroxymethyl) aminomethane


tetraphenyl phosphonium


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Meury, J., Kohiyama, M. ATP is required for K+ active transport in the archaebacterium Haloferax volcanii . Arch. Microbiol. 151, 530–536 (1989).

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Key words

  • Archaebacteria
  • K+ transport
  • Haloferax volcanii