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  Analysis of a putative voltage-gated prokaryotic potassium channel

Unger, D., Barth, A., Haase, W., Kauntzinger, A., Lewitzki, E., Ruiz, T., et al. (2001). Analysis of a putative voltage-gated prokaryotic potassium channel. European Journal of Biochemistry, 268(20), 5386-5396. doi:10.1046/j.0014-2956.2001.02477.x.

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 Creators:
Unger, Daniel1, Author           
Barth, A.2, Author
Haase, Winfried3, Author           
Kauntzinger, A.4, Author
Lewitzki, Erwin5, Author           
Ruiz, Teresa3, Author           
Reiländer, Helmut1, Author           
Michel, Hartmut1, Author           
Affiliations:
1Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
2Institute of Biophysics, Johann Wolfgang Goethe-University, Frankfurt/Main, Germany, ou_persistent22              
3Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
4Institute of Pharmaceutical Chemistry, Johann Wolfgang Goethe-University, Frankfurt/Main, Germany, ou_persistent22              
5Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              

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Free keywords: E. coli Kch; membrane protein; overexpression; potassium channel; purification
 Abstract: Most of the completely sequenced prokaryotic genomes contain genes of potassium channel homologues, but there is still not much known about the role of these proteins in prokaryotes. Here we describe the large-scale overproduction and purification of a prokaryotic voltage-gated potassium channel homologue, Kch, from Escherichia coli. After successful overproduction of the protein, a specific increase in the potassium permeability of the cells was found. Kch could be purified in large amounts using classical purification methods to prevent aggregation of the protein. The physiological state of the protein was revealed to be a homotetramer and the protein was shown to be localized to the cytoplasmic membrane of the cells. In the course of the localization studies, we found a specific increase in the density of the cytoplasmic membrane on Kch production. This was linked to the observed increase in the protein to lipid ratio in the membranes. Another observed change in the membrane composition was an increase in the cardiolipin to phosphatidylglycerol ratio, which may indicate a specific cardiolipin requirement of Kch. On the basis of some of our results, we discuss a function for Kch in the maintenance of the membrane potential in E. coli.

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Language(s): eng - English
 Dates: 2001-08-172001-05-182001-08-222001-12-202001-10-01
 Publication Status: Published in print
 Pages: 11
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1046/j.0014-2956.2001.02477.x
PMID: 11606201
 Degree: -

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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 268 (20) Sequence Number: - Start / End Page: 5386 - 5396 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040