English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Species differences in bacterial NhaA Na+/H+ exchangers

Calinescu, O., Danner, E., Böhm, M., Hunte, C., & Fendler, K. (2014). Species differences in bacterial NhaA Na+/H+ exchangers. FEBS Letters, 588(17), 3111-3116. doi:10.1016/j.febslet.2014.05.066.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Calinescu, Octavian1, Author           
Danner, Eva1, Author           
Böhm, Marc2, Author           
Hunte, Carola3, Author
Fendler, Klaus1, Author           
Affiliations:
1Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society, ou_2068289              
2Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068290              
3Institute for Biochemistry and Molecular Biology, ZBMZ, BIOSS Centre for Biological Signalling Studies, University of Freiburg, Freiburg, Germany, ou_persistent22              

Content

show
hide
Free keywords: NhaA; Cation/proton antiport; Solid supported membrane; Helicobacter pylori; Escherichia coli; Salmonella typhimurium
 Abstract: Bacteria have adapted their NhaA Na+/H+ exchangers responsible for salt homeostasis to their different habitats. We present an electrophysiological and kinetic analysis of NhaA from Helicobacter pylori and compare it to the previously investigated exchangers from Escherichia coli and Salmonella typhimurium. Properties of all three transporters are described by a simple model using a single binding site for H+ and Na+. We show that H. pylori NhaA only has a small acidic shift of its pH-dependent activity profile compared to the other transporters and discuss why a more drastic change in its pH activity profile is not physiologically required.

Details

show
hide
Language(s): eng - English
 Dates: 201420142014-08-25
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.febslet.2014.05.066
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 588 (17) Sequence Number: - Start / End Page: 3111 - 3116 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501