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C400417200v1
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Papers In Press, published online ahead of print September 23, 2004
J. Biol. Chem, 10.1074/jbc.C400417200
Submitted on September 9, 2004
Revised on September 23, 2004
Accepted on September 23, 2004

Functional characterization of a prokaryotic Kir channel

Decha Enkvetchakul, Jaya Bhattacharyya, Iana Jeliazkova, Darcy K. Groesbeck, Catherine A. Cukras, and Colin G. Nichols

Cell Biology and Physiology, Washington University, St. Louis, MO 63110

Corresponding Author: cnichols{at}cellbio.wustl.edu

The Kir gene family encodes inward rectifying K+ (Kir) channels that are widespread and critical regulators of excitability in eukaryotic cells. A related gene family (KirBac) has recently been identified in prokaryotes. While a crystal structure of one member, KirBac1.1, has been solved, there has been no functional characterization of any KirBac gene products. Here we present functional characterization of KirBac1.1 reconstituted in liposomes. Utilizing a 86Rb+ uptake assay, we demonstrate that KirBac1.1 generates a K+-selective permeation path that is inhibited by extraliposomal Ba2+ and Ca2+ ions. In contrast to KcsA (an acid-activated bacterial K channel), KirBac1.1 is inhibited by extraliposomal acid (pK ~6). This characterization of KirBac1.1 activity now paves the way for further correlation of structure and function in this model Kir channel.


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