MjK1, a K+ channel from M. jannaschii, mediates K+ uptake and K+ sensitivity in E. coli

Research output: Contribution to journalArticleResearchpeer review

Authors

  • Jens Hellmer
  • Carsten Zeilinger

External Research Organisations

  • Akademische Fliegergruppe der Universität Hannover e.V.
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Details

Original languageEnglish
Pages (from-to)165-9
Number of pages5
JournalFEBS letters
Volume547
Issue number1-3
Publication statusPublished - 17 Jul 2003

Abstract

The methanogenic and hyperthermophilic deep-sea archaeon Methanococcus jannaschii has three putative K+ channels, MVP (Mj0139), MjK1 (Mj0138.1) and MjK2 (Mj1357). The physiological function of these K+ channels was examined in a viability assay, using the Escherichia coli mutant LB2003 (kup1, DeltakdpABC5, DeltatrkA). While MjK2 expression had no effects on the potassium-dependent phenotype of LB2003, MVP and MjK1 complemented the deficiency at a concentration of 1 mM KCl. In contrast to KcsA, MthK and MVP, MjK1 strongly affected host cell viability at 10 and 100 mM KCl. The toxic effects were less pronounced when growth media were supplemented with the K+ channel blocker BaCl2.

Keywords

    Amino Acid Sequence, Base Sequence, Cell Membrane/physiology, Cloning, Molecular, DNA Primers, Escherichia coli/genetics, Kinetics, Methanococcus/genetics, Molecular Sequence Data, Potassium/metabolism, Potassium Channels/chemistry, Recombinant Proteins/chemistry, Sequence Alignment, Sequence Homology, Amino Acid

Cite this

MjK1, a K+ channel from M. jannaschii, mediates K+ uptake and K+ sensitivity in E. coli. / Hellmer, Jens; Zeilinger, Carsten.
In: FEBS letters, Vol. 547, No. 1-3, 17.07.2003, p. 165-9.

Research output: Contribution to journalArticleResearchpeer review

Hellmer J, Zeilinger C. MjK1, a K+ channel from M. jannaschii, mediates K+ uptake and K+ sensitivity in E. coli. FEBS letters. 2003 Jul 17;547(1-3):165-9. doi: 10.1016/s0014-5793(03)00706-3
Hellmer, Jens ; Zeilinger, Carsten. / MjK1, a K+ channel from M. jannaschii, mediates K+ uptake and K+ sensitivity in E. coli. In: FEBS letters. 2003 ; Vol. 547, No. 1-3. pp. 165-9.
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abstract = "The methanogenic and hyperthermophilic deep-sea archaeon Methanococcus jannaschii has three putative K+ channels, MVP (Mj0139), MjK1 (Mj0138.1) and MjK2 (Mj1357). The physiological function of these K+ channels was examined in a viability assay, using the Escherichia coli mutant LB2003 (kup1, DeltakdpABC5, DeltatrkA). While MjK2 expression had no effects on the potassium-dependent phenotype of LB2003, MVP and MjK1 complemented the deficiency at a concentration of 1 mM KCl. In contrast to KcsA, MthK and MVP, MjK1 strongly affected host cell viability at 10 and 100 mM KCl. The toxic effects were less pronounced when growth media were supplemented with the K+ channel blocker BaCl2.",
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AU - Zeilinger, Carsten

N1 - Funding information: We are grateful to Prof. E. Bakker for providing us with E. coli mutant LB2003. We thank M. Kieß (GBF, Braunschweig, Germany) for amino acid sequencing. We also thank Henri Tietge and Ramani Balasubramanian for proofreading. This project was supported by the FSP, Lower Saxony Agrar Biotechnology subproject CZ.

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N2 - The methanogenic and hyperthermophilic deep-sea archaeon Methanococcus jannaschii has three putative K+ channels, MVP (Mj0139), MjK1 (Mj0138.1) and MjK2 (Mj1357). The physiological function of these K+ channels was examined in a viability assay, using the Escherichia coli mutant LB2003 (kup1, DeltakdpABC5, DeltatrkA). While MjK2 expression had no effects on the potassium-dependent phenotype of LB2003, MVP and MjK1 complemented the deficiency at a concentration of 1 mM KCl. In contrast to KcsA, MthK and MVP, MjK1 strongly affected host cell viability at 10 and 100 mM KCl. The toxic effects were less pronounced when growth media were supplemented with the K+ channel blocker BaCl2.

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KW - Base Sequence

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KW - DNA Primers

KW - Escherichia coli/genetics

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KW - Methanococcus/genetics

KW - Molecular Sequence Data

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KW - Recombinant Proteins/chemistry

KW - Sequence Alignment

KW - Sequence Homology, Amino Acid

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