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Identification of the arginine/ornithine antiporter ArcD from Halobacterium salinarum
Author(s) -
Wimmer Florian,
Oberwinkler Tanja,
Bisle Birgit,
Tittor Jörg,
Oesterhelt Dieter
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.10.004
Subject(s) - halobacterium salinarum , arginine , antiporter , chemistry , biochemistry , agmatine , identification (biology) , ornithine , biology , bacteriorhodopsin , botany , amino acid , membrane
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 ΔArcD 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 34 kD protein is the functional unit.