Identification of the arginine/ornithine antiporter ArcD from Halobacterium salinarum.

Florian Wimmer, Tanja Oberwinkler, Birgit Bisle, Jörg Tittor, Dieter Oesterhelt

Journal: FEBS letters 2009;582(27):3771-5

PMID: 18930051

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.

Address: Department of Membrane Biochemistry, Max Planck Institut for Biochemistry, Am Klopferspitz 18, D82152 Martinsried, Germany.

Link outs

Subscription / membership required

Bant logo

© Copyright 2026, Nutrition Evidence

NED wishes to thank the following organisations for their support:

We use cookies to improve your experience and analyze site traffic with Google Analytics. By continuing to use our site, you agree to our use of cookies. Learn more.