Residue Aspartate-147 from the Third Transmembrane Region of Na + /H + Antiporter NhaB of Vibrio alginolyticus Plays a Role in Its Activity
Open Access
- 1 October 2001
- journal article
- research article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 183 (19) , 5762-5767
- https://doi.org/10.1128/jb.183.19.5762-5767.2001
Abstract
NhaB is a bacterial Na + /H + antiporter with unique topology. The pH dependence of NhaB from Vibrio alginolyticus differs from that of the Escherichia coli NhaB homolog. Replacement of Asp-147 with Glu made high H + concentrations a requirement for the NhaB activity. Replacement of Asp-147 with neutral amino acids inactivated NhaB.Keywords
This publication has 28 references indexed in Scilit:
- Three-dimensional structure of the ion-coupled transport protein NhaANature, 2000
- Topological Analysis of NhaA, a Na+/H+ Antiporter from Escherichia coliJournal of Biological Chemistry, 1996
- Cloning and sequencing of the nhaB gene encoding an Na+/H+ antiporter from Vibrio alginolyticusBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1996
- Chapter 22 Bacterial Na+/H+ antiporters — Molecular biology, biochemistry and physiologyPublished by Elsevier ,1996
- Identification of Strong Modifications in Cation Selectivity in an Arabidopsis Inward Rectifying Potassium Channel by Mutant Selection in YeastPublished by Elsevier ,1995
- Three aspartic residues in membrane-spanning regions of Na+/H+ antiporter from Vibrio alginolyticus play a role in the activity of the carrierBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1995
- Genetic Evidence for Two Sequentially Occupied K+ Binding Sites in the Kdp Transport ATPaseJournal of Biological Chemistry, 1995
- Cloning and sequencing of an Na+/H+ antiporter gene from the marine bacterium Vibrio alginolyticusBiochimica et Biophysica Acta (BBA) - Biomembranes, 1994
- pHG165: A pBR322 copy number derivative of pUC8 for cloning and expressionPlasmid, 1986
- Effects of pH and monovalent cations on the potassium ion exit from the marine bacterium, Vibrio alginolyticus, and the manipulation of cellular cation contentsBiochimica et Biophysica Acta (BBA) - Biomembranes, 1982