The Journal of General Physiology
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Published 27 August 2001. doi:10.1085/jgp.118.3.303
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© The Rockefeller University Press, 0022-1295/2001/9/303/ $5.00
The Journal of General Physiology, Volume 118, Number 3, September 1, 2001 303-314


Original Article

KcsA: It's a Potassium Channel

Meredith LeMasuriera, Lise Heginbothama, and Christopher Millera
a Department of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, MA 02454

Correspondence to: Christopher Miller, Department of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, MA 02454. Fax:(781) 736-2365 E-mail:cmiller{at}brandeis.edu.

Ion conduction and selectivity properties of KcsA, a bacterial ion channel of known structure, were studied in a planar lipid bilayer system at the single-channel level. Selectivity sequences for permeant ions were determined by symmetrical solution conductance (K+ > Rb+, NH4+, Tl+ >> Cs+, Na+, Li+) and by reversal potentials under bi-ionic or mixed-ion conditions (Tl+ > K+ > Rb+ > NH4+ >> Na+, Li+). Determination of reversal potentials with submillivolt accuracy shows that K+ is over 150-fold more permeant than Na+. Variation of conductance with concentration under symmetrical salt conditions is complex, with at least two ion-binding processes revealing themselves: a high affinity process below 20 mM and a low affinity process over the range 100–1,000 mM. These properties are analogous to those seen in many eukaryotic K+ channels, and they establish KcsA as a faithful structural model for ion permeation in eukaryotic K+ channels.

Key Words: ion conductivity, selectivity


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