PMID:12740360
| Citation |
Steuber, J (2003) The C-terminally truncated NuoL subunit (ND5 homologue) of the Na+-dependent complex I from Escherichia coli transports Na+. J. Biol. Chem. 278:26817-22 |
|---|---|
| Abstract |
The NADH:quinone oxidoreductase (complex I) from Escherichia coli acts as a primary Na+ pump. Expression of a C-terminally truncated version of the hydrophobic NuoL subunit (ND5 homologue) from E. coli complex I resulted in Na+-dependent growth inhibition of the E. coli host cells. Membrane vesicles containing the truncated NuoL subunit (NuoLN) exhibited 2-4-fold higher Na+ uptake activity than control vesicles without NuoLN. Respiratory proton transport into inverted vesicles containing NuoLN decreased upon addition of Na+, but was not affected by K+, indicating a Na+-dependent increase of proton permeability of membranes in the presence of NuoLN. The His-tagged NuoLN protein was solubilized, enriched by affinity chromatography, and reconstituted into proteoliposomes. Reconstituted His6-NuoLN facilitated the uptake of Na+ into the proteoliposomes along a concentration gradient. This Na+ uptake was prevented by EIPA (5-(N-ethyl-N-isopropyl)-amiloride), which acts as inhibitor against Na+/H+ antiporters. |
| Links |
PubMed Online version:10.1074/jbc.M301682200 |
| Keywords |
Base Sequence; Cell Membrane Permeability; DNA, Bacterial/genetics; Electron Transport Complex I; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Ion Transport; Kinetics; Models, Biological; Models, Molecular; NADH, NADPH Oxidoreductases/chemistry; NADH, NADPH Oxidoreductases/genetics; NADH, NADPH Oxidoreductases/metabolism; Protein Subunits; Proton Pumps/chemistry; Proton Pumps/genetics; Proton Pumps/metabolism; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Sequence Deletion; Sodium/metabolism |
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