Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 232-41 |
| Seitenumfang | 10 |
| Fachzeitschrift | The EMBO journal |
| Jahrgang | 26 |
| Ausgabenummer | 1 |
| Publikationsstatus | Veröffentlicht - 10 Jan. 2007 |
Abstract
To date, the biological role of prokaryotic K(+) channels remains unknown. Helicobacter pylori contains a gene encoding a putative K(+) channel (HpKchA) of the two-transmembrane RCK (regulation of K(+) conductance) domain family, but lacks known bacterial K(+) uptake systems. A H. pylori DeltahpKchA mutant presented a strong growth defect at low K(+) concentration, which was compensated by KCl addition. The role of the separate RCK domain was investigated in H. pylori by mutagenesis of its internal start codon, which led to a K(+)-dependent intermediate growth phenotype, consistent with RCK activating channel function. Tagging HpKchA C-terminally, we detected a 1:1 stoichiometry of the full-length HpKchA and the separate RCK domain. We constructed single amino-acid exchanges within the unusual selectivity filter of HpKchA (ATGFGA) in H. pylori and observed complete loss (G74A), a slight defect (G76A or F75G) or wild-type (A77D) channel function. HpKchA was essential for colonization of the murine stomach. These data show, for the first time, a biological function for a prokaryotic K(+) channel, as a K(+) uptake system, essential for the persistence of H. pylori in the gastric environment.
Zitieren
- Standard
- Harvard
- Apa
- Vancouver
- BibTex
- RIS
in: The EMBO journal, Jahrgang 26, Nr. 1, 10.01.2007, S. 232-41.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Channel-mediated potassium uptake in Helicobacter pylori is essential for gastric colonization
AU - Stingl, Kerstin
AU - Brandt, Sonja
AU - Uhlemann, Eva-Maria
AU - Schmid, Roland
AU - Altendorf, Karlheinz
AU - Zeilinger, Carsten
AU - Ecobichon, Chantal
AU - Labigne, Agnès
AU - Bakker, Evert P
AU - de Reuse, Hilde
PY - 2007/1/10
Y1 - 2007/1/10
N2 - To date, the biological role of prokaryotic K(+) channels remains unknown. Helicobacter pylori contains a gene encoding a putative K(+) channel (HpKchA) of the two-transmembrane RCK (regulation of K(+) conductance) domain family, but lacks known bacterial K(+) uptake systems. A H. pylori DeltahpKchA mutant presented a strong growth defect at low K(+) concentration, which was compensated by KCl addition. The role of the separate RCK domain was investigated in H. pylori by mutagenesis of its internal start codon, which led to a K(+)-dependent intermediate growth phenotype, consistent with RCK activating channel function. Tagging HpKchA C-terminally, we detected a 1:1 stoichiometry of the full-length HpKchA and the separate RCK domain. We constructed single amino-acid exchanges within the unusual selectivity filter of HpKchA (ATGFGA) in H. pylori and observed complete loss (G74A), a slight defect (G76A or F75G) or wild-type (A77D) channel function. HpKchA was essential for colonization of the murine stomach. These data show, for the first time, a biological function for a prokaryotic K(+) channel, as a K(+) uptake system, essential for the persistence of H. pylori in the gastric environment.
AB - To date, the biological role of prokaryotic K(+) channels remains unknown. Helicobacter pylori contains a gene encoding a putative K(+) channel (HpKchA) of the two-transmembrane RCK (regulation of K(+) conductance) domain family, but lacks known bacterial K(+) uptake systems. A H. pylori DeltahpKchA mutant presented a strong growth defect at low K(+) concentration, which was compensated by KCl addition. The role of the separate RCK domain was investigated in H. pylori by mutagenesis of its internal start codon, which led to a K(+)-dependent intermediate growth phenotype, consistent with RCK activating channel function. Tagging HpKchA C-terminally, we detected a 1:1 stoichiometry of the full-length HpKchA and the separate RCK domain. We constructed single amino-acid exchanges within the unusual selectivity filter of HpKchA (ATGFGA) in H. pylori and observed complete loss (G74A), a slight defect (G76A or F75G) or wild-type (A77D) channel function. HpKchA was essential for colonization of the murine stomach. These data show, for the first time, a biological function for a prokaryotic K(+) channel, as a K(+) uptake system, essential for the persistence of H. pylori in the gastric environment.
KW - Amino Acid Sequence
KW - Animals
KW - Codon, Initiator
KW - Cytoplasm/metabolism
KW - Gastric Mucosa/microbiology
KW - Helicobacter pylori/metabolism
KW - Hydrogen-Ion Concentration
KW - Mice
KW - Models, Biological
KW - Molecular Sequence Data
KW - Potassium/chemistry
KW - Potassium Channels/chemistry
KW - Protein Structure, Tertiary
KW - Sequence Homology, Amino Acid
U2 - 10.1038/sj.emboj.7601471
DO - 10.1038/sj.emboj.7601471
M3 - Article
C2 - 17159901
VL - 26
SP - 232
EP - 241
JO - The EMBO journal
JF - The EMBO journal
SN - 0261-4189
IS - 1
ER -