This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bertrand, J.
Right arrow Articles by Bramkamp, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bertrand, J.
Right arrow Articles by Bramkamp, M.

 Previous Article  |  Next Article 

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,{dagger} Karlheinz Altendorf,* and Marc Bramkamp{ddagger}

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.

* Corresponding author. Mailing address: Abteilung Mikrobiologie, Fachbereich Biologie/Chemie, Universität Osnabrück, Barbarastraße 11, D-49076 Osnabrück, Germany. Phone: 49-541-969-2864. Fax: 49-541-969-12891. E-mail: Altendorf{at}biologie.uni-osnabrueck.de.

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

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

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.



This article has been cited by other articles:

  • Haupt, M., Bramkamp, M., Heller, M., Coles, M., Deckers-Hebestreit, G., Herkenhoff-Hesselmann, B., Altendorf, K., Kessler, H. (2006). The Holo-form of the Nucleotide Binding Domain of the KdpFABC Complex from Escherichia coli Reveals a New Binding Mode. J. Biol. Chem. 281: 9641-9649 [Abstract] [Full Text]  
  • Tholema, N., Bruggen, M. V. d., Maser, P., Nakamura, T., Schroeder, J. I., Kobayashi, H., Uozumi, N., Bakker, E. P. (2005). All Four Putative Selectivity Filter Glycine Residues in KtrB Are Essential for High Affinity and Selective K+ Uptake by the KtrAB System from Vibrio alginolyticus. J. Biol. Chem. 280: 41146-41154 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»