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Journal of Bacteriology, August 2004, p. 5519-5522, Vol. 186, No. 16
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.16.5519-5522.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Amino Acid Substitutions in Putative Selectivity Filter Regions III and IV in KdpA Alter Ion Selectivity of the KdpFABC Complex from Escherichia coli

Jessica Bertrand, Karlheinz Altendorf,^* and Marc Bramkamp

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

Received 5 May 2004/ Accepted 6 May 2004

When grown under conditions of potassium limitation or high osmolality, Escherichia coli synthesizes the K⁺-translocating KdpFABC complex. The KdpA subunit, which has sequence homology to potassium channels of the KcsA type, has been shown to be important for potassium binding and transport. Replacement of the glycine residues in KdpA at positions 345 and 470, members of putative selectivity filter regions III and IV, alters the ion selectivity of the KdpFABC complex.

Present address: Arterioskleroseforschung, Abteilung molekulare Kardiologie, Uniklinikum Münster, 48149 Münster, Germany.

Present address: Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.

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