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© The Rockefeller University Press, 0022-1295/1998//741/ $5.00
Journal of General Physiology, Volume 111, Number 6, 1998

Article

Functional Reconstitution of a Prokaryotic K+ Channel

Lise Heginbotham, Ludmila Kolmakova-Partensky, and Christopher Miller

From the Department of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02254

SliK, a K+ channel encoded by the Streptomyces KcsA gene, was expressed, purified, and reconstituted in liposomes. A concentrative 86Rb+ flux assay was used to assess the ion transport properties of SliK. SliK-mediated ionic flux shows strong selectivity for K+ over Na+ and is inhibited by micromolar concentrations of Ba2+, mirroring the basic permeation characteristic of eukaryotic K+ channels studied by electrophysiological methods. 86Rb+ uptake kinetics and equilibrium measurements also demonstrate that the purified protein is fully active.

Key Words: liposome • conduction • selectivity • flux

Address correspondence to Christopher Miller, Department of Biochemistry, Howard Hughes Medical Institute, Brandeis University, 415 South Street, HHMI, Waltham, Massachusetts 02254. Fax: 781-736-2365; E-mail: cmiller{at}brandeis.edu

Abbreviations: CL, bovine heart cardiolipin; NMG, N--methylglucamine; PE, E. coli phosphatidylethanolamine; PG, egg phosphatidylglycerol


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