PubMed 10539975
Referenced in: none
Automatically associated channels: ClC4
Title: High-level expression, functional reconstitution, and quaternary structure of a prokaryotic ClC-type chloride channel.
Authors: M Maduke, D J Pheasant, C Miller
Journal, date & volume: J. Gen. Physiol., 1999 Nov , 114, 713-22
PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/10539975
Abstract
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.