Isolation and characterization of the high-affinity K(+)-translocating ATPase from Rhodobacter sphaeroides

Author:

Abee T1,Siebers A1,Altendorf K1,Konings W N1

Affiliation:

1. Department of Microbiology, University of Groningen, Haren, The Netherlands.

Abstract

Cells of the purple nonsulfur bacterium Rhodobacter sphaeroides express a high-affinity K+ uptake system when grown in media with low K+ concentrations. A vanadate-sensitive, K(+)-stimulated and Mg(2+)-stimulated ATPase was purified from membranes of these cells by solubilization with decyl-beta-D-maltoside in the presence of Escherichia coli phospholipids followed by triazine-dye affinity chromatography. This primary transport system has a substrate specificity and an inhibitor sensitivity closely similar to those of the Kdp ATPase from E. coli and is composed of three subunits with molecular masses of 70.0, 43.5, and 23.5 kDa.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference44 articles.

1. Abee T. E. P. Bakker K. J. Heliingwerf and W. N. Konings. 1990. Potassium transport in Rhodobacter sphaeroides. Sixth European Bioenergetics Conference Short Reports 6:C.IV-22.

2. Effects of potassium ions on proton motive force in Rhodobacter sphaeroides;Abee T.;J. Bacteriol.,1988

3. The relation between electron transfer, proton motive force and lactose transport in membrane vesicles from aerobically grown Rhodobacter sphaeroides;Abee T.;Biochim. Biophys. Acta,1988

4. Abee T. J. Knol K. J. Hellingwerf E. P. Bakker A. Siebers and W. N. Konings. Submitted for publication.

5. Osmoregulation in Rhodobactersphaeroides;Abee T.;J. Bacteriol.,1990

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