» Articles » PMID: 7489706

A Prokaryotic Potassium Ion Channel with Two Predicted Transmembrane Segments from Streptomyces Lividans

Overview
Journal EMBO J
Date 1995 Nov 1
PMID 7489706
Citations 107
Authors
Affiliations
Soon will be listed here.
Abstract

We report the identification, functional expression, purification, reconstitution and electrophysiological characterization of an up to now unique prokaryotic potassium ion channel (KcsA). It has a rectifying current-voltage relationship and displays subconductance states, the largest of which amounts to A approximately equal to 90 pS. The channel is blocked by Cs- ions and gating requires the presence of Mg2+ ions. The kcsA gene has been identified in the gram-positive soil bacterium Streptomyces lividans. It encodes a predicted 17.6 kDa protein with two potential membrane-spanning helices linked by a central domain which shares a high degree of similarity with the H5 segment conserved among eukaryotic ion channels. Multiple alignments of deduced amino acids suggest that the novel channel has the closest kinship to the S5, H5 and S6 regions of voltage-gated K+ channel families, mainly to the subfamily represented by the Shaker protein from Drosophila melanogaster. Moreover, KcsA is most distantly related to eukaryotic inwardly rectifying channels with two putative predicted transmembrane segments.

Citing Articles

pH-induced conformational changes in the selectivity filter of a potassium channel lead to alterations in its selectivity and permeation properties.

Coll-Diez C, Giudici A, Potenza A, Gonzalez-Ros J, Poveda J Front Pharmacol. 2025; 15():1499383.

PMID: 39834826 PMC: 11743430. DOI: 10.3389/fphar.2024.1499383.


Conformational Dynamic Studies of Prokaryotic Potassium Channels Explored by Homo-FRET Methodologies.

Coutinho A, Poveda J, Renart M Methods Mol Biol. 2024; 2796:35-72.

PMID: 38856894 DOI: 10.1007/978-1-0716-3818-7_3.


Insights into potassium channel family and their biological functions.

Paul A, Chumbale S, Lakra A, Kumar V, Alhat D, Singh S 3 Biotech. 2023; 13(8):266.

PMID: 37425093 PMC: 10326225. DOI: 10.1007/s13205-023-03692-y.


Osmotic stress responses and the biology of the second messenger c-di-AMP in .

Bhowmick S, Shenouda M, Tschowri N Microlife. 2023; 4:uqad020.

PMID: 37223731 PMC: 10117811. DOI: 10.1093/femsml/uqad020.


Mechanisms and physiological implications of cooperative gating of clustered ion channels.

Dixon R, Navedo M, Binder M, Santana L Physiol Rev. 2021; 102(3):1159-1210.

PMID: 34927454 PMC: 8934683. DOI: 10.1152/physrev.00022.2021.


References
1.
Dower W, Miller J, Ragsdale C . High efficiency transformation of E. coli by high voltage electroporation. Nucleic Acids Res. 1988; 16(13):6127-45. PMC: 336852. DOI: 10.1093/nar/16.13.6127. View

2.
Mueller P, RUDIN D, Tien H, WESCOTT W . Reconstitution of cell membrane structure in vitro and its transformation into an excitable system. Nature. 1962; 194:979-80. DOI: 10.1038/194979a0. View

3.
Patlak J . Sodium channel subconductance levels measured with a new variance-mean analysis. J Gen Physiol. 1988; 92(4):413-30. PMC: 2228911. DOI: 10.1085/jgp.92.4.413. View

4.
Pigac J, Vujaklija D, Toman Z, Gamulin V, Schrempf H . Structural instability of a bifunctional plasmid pZG1 and single-stranded DNA formation in Streptomyces. Plasmid. 1988; 19(3):222-30. DOI: 10.1016/0147-619x(88)90040-6. View

5.
Kessler A, Dittrich W, Betzler M, Schrempf H . Cloning and analysis of a deletable tetracycline-resistance determinant of Streptomyces lividans 1326. Mol Microbiol. 1989; 3(8):1103-9. DOI: 10.1111/j.1365-2958.1989.tb00260.x. View