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Published online 25 October 1999.
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© The Rockefeller University Press, 0022-1295/1999/11/713/ $5.00
The Journal of General Phyiology, Volume 114, Number 5, November 1, 1999 713-722

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

Correspondence to: Christopher Miller, Department of Biochemistry, Brandeis University, 415 South Street, HHMI, Waltham, MA 02254-9110. Fax:781-736-2365 E-mail:cmiller{at}brandeis.edu.

Released online: 25 October 1999

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


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