The Na+/H+ antiporter of the thermohalophilic bacterium Rhodothermus marinus

Biochem Biophys Res Commun. 2006 Sep 29;348(3):1011-7. doi: 10.1016/j.bbrc.2006.07.134. Epub 2006 Jul 31.

Abstract

In the thermohalophilic bacterium Rhodothermus marinus, the NADH:quinone oxidoreductase (complex I) is encoded by two single genes and two operons, one of which contains the genes for five complex I subunits, nqo10-nqo14, a pterin carbinolamine dehydratase, and a putative single subunit Na+/H+ antiporter. Here we report that the latter encodes indeed a functional Na+/H+ antiporter, which is able to confer resistance to Na+, but not to Li+ to an Escherichia coli strain defective in Na+/H+ antiporters. In addition, an extensive amino acid sequence comparison with several single subunit Na+/H+ antiporters from different groups, namely NhaA, NhaB, NhaC, and NhaD, suggests that this might be the first member of a new type of Na+/H+ antiporters, which we propose to call NhaE.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Electron Transport Complex I / chemistry
  • Electron Transport Complex I / physiology
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / physiology
  • Gene Expression Regulation, Bacterial
  • Hydrogen-Ion Concentration
  • Molecular Sequence Data
  • Rhodothermus / chemistry*
  • Rhodothermus / physiology*
  • Sodium-Hydrogen Exchangers / biosynthesis
  • Sodium-Hydrogen Exchangers / chemistry*
  • Sodium-Hydrogen Exchangers / genetics
  • Sodium-Hydrogen Exchangers / physiology*
  • Transcription, Genetic / physiology

Substances

  • Escherichia coli Proteins
  • NhaA protein, E coli
  • Sodium-Hydrogen Exchangers
  • Electron Transport Complex I