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Updated: Jun 28, 2026

Characterization of Membrane Transporters by Heterologous Expression in E. coli and Production of Membrane Vesicles
Published on: December 31, 2019
Identification of the arginine/ornithine antiporter ArcD from Halobacterium salinarum
Florian Wimmer1, Tanja Oberwinkler, Birgit Bisle
1Department of Membrane Biochemistry, Max Planck Institut for Biochemistry, Am Klopferspitz 18, D82152 Martinsried, Germany.
Abstract:
This paper identifies the first arginine/ornithine antiporter ArcD from the domain of archea. The functional role of ArcD is demonstrated by transport assays with radioactive labelled arginine, by its necessity to enable arginine fermentation under anaerobic growth conditions and by the consumption of arginine from the medium during growth. All three experimentally observables are severely disturbed when the deletion strain DeltaArcD is used. The isolated protein is verified by mass spectrometry and reconstituted in vesicles. The proteoliposomes are attached to a membrane and capacitive currents are recorded which appear upon initiation of the transport process by change from arginine-free to arginine-containing buffer. This clearly demonstrates that the purified 34kD protein is the functional unit.
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