Characterization of Amino Acid Substitutions in KdpA, the K + -Binding and -Translocating Subunit of the KdpFABC Complex of Escherichia coli

Author:

van der Laan Martin1,Gaßel Michael1,Altendorf Karlheinz1

Affiliation:

1. Abteilung Mikrobiologie, Fachbereich Biologie/Chemie, Universität Osnabrück, D-49069 Osnabrück, Germany

Abstract

ABSTRACT When grown under K + limitation, Escherichia coli induces the K + -translocating KdpFABC complex. The stimulation of ATPase activity by NH 4 + ions was shown for the first time. Substitutions in KdpA, which is responsible for K + binding and translocation, revealed that enzyme complexes KdpA:G232A and KdpA:G232S have completely lost their cation selectivity.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference23 articles.

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2. Altendorf K. M. Gaßel W. Puppe T. Möllenkamp A. Zeeck C. Boddien K. Fendler E. Bamberg and S. Dröse. 1998. Structure and function of the Kdp-ATPase of Escherichia coli . Acta Physiol. Scand. 163 (Suppl.) : 137-146.

3. Buurman, E. T., K.-T. Kim, and W. Epstein. 1995. Genetic evidence of two sequentially occupied K+ binding sites in the Kdp transport ATPase. J. Biol. Chem.270:6678-6685.

4. Buurman, E. T., M. J. Teixera de Mattos, and O. M. Neijssel. 1991. Futile cycling of ammonium ions via the high affinity potassium uptake system (Kdp) of Escherichia coli. Arch. Microbiol.155:391-395.

5. Dorus, S., H. Mimaru, and W. Epstein. 2001. Substrate-binding clusters of the K+-transporting Kdp ATPase of Escherichia coli investigated by amber suppression scanning mutagenesis. J. Biol. Chem.276:9590-9598.

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