The Escherichia coli AmtB protein as a model system for understanding ammonium transport by Amt and Rh proteins

Translated title of the contribution: La protéine AmtB de Escherichia coli, un sytème modèle pour la compréhension du transport d'ammonium par AmtB et les protéines Rh

M Merrick, A Javelle, A Durand, E Severi, J Thornton, N D Avent, M J Conroy, P A Bullough

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

The Escherichia coli ammonium transport protein (AmtB) has become the model system of choice for analysis of the process of ammonium uptake by the ubiquitous Amt family of inner membrane proteins. Over the past 6 years we have developed a range of genetic and biochemical tools in this system. These have allowed structure/function analysis to develop rapidly, offering insight initially into the membrane topology of the protein and most recently leading to the solution of high-resolution 3D structures. Genetic analysis has revealed a novel regulatory mechanism that is apparently conserved in prokaryotic Amt proteins and genetic approaches are also now being used to dissect structure/function relationships in Amt proteins. The now well-recognised homology between the Amt proteins, found in archaea, eubacteria, fungi and plants, and the Rhesus proteins, found characteristically in animals, also means that studies on E. coli AmtB can potentially shed light on structure/function relationships in the clinically important Rh proteins.

Translated title of the contributionLa protéine AmtB de Escherichia coli, un sytème modèle pour la compréhension du transport d'ammonium par AmtB et les protéines Rh
Original languageMultiple languages
Pages (from-to)97-102
Number of pages6
JournalTransfusion clinique et biologique : journal de la Société française de transfusion sanguine
Volume13
Issue number1-2
DOIs
Publication statusPublished - 28 Mar 2006

Keywords

  • ammonia
  • biological transport
  • blood proteins
  • cation transport proteins
  • Escherichia coli proteins
  • gene expression regulation
  • humans
  • membrane glycoproteins
  • models, molecular
  • nucleotidyltransferases
  • PII nitrogen regulatory proteins
  • protein conformation
  • quaternary ammonium compounds
  • Rh-Hr blood-group system
  • saccharomyces cerevisiae proteins
  • signal transduction
  • species specificity
  • structure-activity relationship
  • substrate specificity

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