Functional Reconstitution of a Prokaryotic K(+) Channel

SliK, a K(+) channel encoded by the Streptomyces KcsA gene, was expressed, purified, and reconstituted in liposomes. A concentrative (86)Rb(+) flux assay was used to assess the ion transport properties of SliK. SliK-mediated ionic flux shows strong selectivity for K(+) over Na(+) and is inhibited by...

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Autores principales: Heginbotham, Lise, Kolmakova-Partensky, Ludmila, Miller, Christopher
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1998
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2217152/
https://www.ncbi.nlm.nih.gov/pubmed/9607934
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author Heginbotham, Lise
Kolmakova-Partensky, Ludmila
Miller, Christopher
author_facet Heginbotham, Lise
Kolmakova-Partensky, Ludmila
Miller, Christopher
author_sort Heginbotham, Lise
collection PubMed
description SliK, a K(+) channel encoded by the Streptomyces KcsA gene, was expressed, purified, and reconstituted in liposomes. A concentrative (86)Rb(+) flux assay was used to assess the ion transport properties of SliK. SliK-mediated ionic flux shows strong selectivity for K(+) over Na(+) and is inhibited by micromolar concentrations of Ba(2+), mirroring the basic permeation characteristic of eukaryotic K(+) channels studied by electrophysiological methods. (86)Rb(+) uptake kinetics and equilibrium measurements also demonstrate that the purified protein is fully active.
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spelling pubmed-22171522008-04-22 Functional Reconstitution of a Prokaryotic K(+) Channel Heginbotham, Lise Kolmakova-Partensky, Ludmila Miller, Christopher J Gen Physiol Article SliK, a K(+) channel encoded by the Streptomyces KcsA gene, was expressed, purified, and reconstituted in liposomes. A concentrative (86)Rb(+) flux assay was used to assess the ion transport properties of SliK. SliK-mediated ionic flux shows strong selectivity for K(+) over Na(+) and is inhibited by micromolar concentrations of Ba(2+), mirroring the basic permeation characteristic of eukaryotic K(+) channels studied by electrophysiological methods. (86)Rb(+) uptake kinetics and equilibrium measurements also demonstrate that the purified protein is fully active. The Rockefeller University Press 1998-06-01 /pmc/articles/PMC2217152/ /pubmed/9607934 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Article
Heginbotham, Lise
Kolmakova-Partensky, Ludmila
Miller, Christopher
Functional Reconstitution of a Prokaryotic K(+) Channel
title Functional Reconstitution of a Prokaryotic K(+) Channel
title_full Functional Reconstitution of a Prokaryotic K(+) Channel
title_fullStr Functional Reconstitution of a Prokaryotic K(+) Channel
title_full_unstemmed Functional Reconstitution of a Prokaryotic K(+) Channel
title_short Functional Reconstitution of a Prokaryotic K(+) Channel
title_sort functional reconstitution of a prokaryotic k(+) channel
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2217152/
https://www.ncbi.nlm.nih.gov/pubmed/9607934
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