The Journal of General Physiology
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Published online 1 November 1999.
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© The Rockefeller University Press, 0022-1295/1999//713/ $5.00
Journal of General Physiology, Volume 114, Number 5, 1999

Original Article

High-Level Expression, Functional Reconstitution, and Quaternary Structure of a Prokaryotic Clc-Type Chloride Channel

Merritt Madukea, Deborah J. Pheasanta, and Christopher Millera

a From the Department of Biochemistry, Howard Hughes Medical Institute, Brandeis University, Waltham, Massachusetts 02254-9110
Department of Biochemistry, Brandeis University, 415 South Street, HHMI, Waltham, MA 02254-9110.781-736-2365

cmiller{at}brandeis.edu

ClC-type anion-selective channels are widespread throughout eukaryotic organisms. BLAST homology searches reveal that many microbial genomes also contain members of the ClC family. An Escherichia coli–derived ClC Cl– channel homologue, "EriC," the product of the yadQ gene, was overexpressed in E. coli and purified in milligram quantities in a single-step procedure. Reconstitution of purified EriC into liposomes confers on these membranes permeability to anions with selectivity similar to that observed electrophysiologically in mammalian ClC channels. Cross-linking studies argue that EriC is a homodimer in both detergent micelles and reconstituted liposomes, a conclusion corroborated by gel filtration and analytical sedimentation experiments.

Key Words: yadQ • liposome • chromatography • glutaraldehyde • ultracentrifugation

© 1999 The Rockefeller University Press


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