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Uncoupling and Turnover in a Cl−/H+ Exchange Transporter
Abstract
The CLC-family protein CLC-ec1, a bacterial homologue of known structure, stoichiometrically exchanges two Cl− for one H+ via an unknown membrane transport mechanism. This study examines mutations at a conserved tyrosine residue, Y445, that directly coordinates a Cl− ion located near the center of the membrane. Mutations at this position lead to “uncoupling,” such that the H+/Cl− transport ratio decreases roughly with the volume of the substituted side chain. The uncoupled proteins are still able to pump protons uphill when driven by a Cl− gradient, but the extent and rate of this H+ pumping is weaker in the more uncoupled variants. Uncoupling is accompanied by conductive Cl− transport that is not linked to counter-movement of H+, i.e., a “leak.” The unitary Cl− transport rate, measured in reconstituted liposomes by both a conventional initial-velocity method and a novel Poisson dilution approach, is ∼4,000 s−1 for wild-type protein, and the uncoupled mutants transport Cl− at similar rates.
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Mutating each of three conserved Bpe residues coordinating the F- densities (F82, F85, N43) did not produce single-channel activity in electrical recordings, but anion-dump experiments reveal dramatic changes in F- permeation.
“We next examined the functional consequences of mutating each of three conserved Bpe residues coordinating the F- densities: F82, F85, and N43. We did not observe single-channel activity in electrical recordings, but more sensitive “anion-dump” experiments22,23 reveal dramatic changes in F- permeation”
From Crystal structures of a double-barrelled fluoride ion channel (2015) · cites this paper as [22]
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Crystal structures of a double-barrelled fluoride ion channel
Stockbridge, R. B., Kolmakova-Partensky, L., Shane, T., Koide, A., Koide, S., Miller, C., & Newstead, S. (2015) · Nature · doi:10.1038/nature14981 · Cited by 119
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Metadata
- Authors
- Walden, M., Accardi, A., Wu, F., Xu, C., Williams, C., & Miller, C.
- Venue
- The Journal of General Physiology
- Publisher
- Rockefeller University Press
- Published
- 2007-03-26
- Volume
- 129
- Issue
- 4
- Pages
- 317-329
- ISSN
- 1540-7748
- 0022-1295
- PMC
- PMC2151619
- Cited by
- 142
- References
- 0
- Language
- en
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