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

• Published in: Transfusion clinique et biologique (Paris) Vol. 13; no. 1; pp. 97 - 102
• Main Authors: Merrick, M., Javelle, A., Durand, A., Severi, E., Thornton, J., Avent, N.D., Conroy, M.J., Bullough, P.A.
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Paris Elsevier SAS 01.03.2006; Elsevier
• Subjects: Ammonia - metabolism; Ammonium transport; AmtB; Anesthesia. Intensive care medicine. Transfusions. Cell therapy and gene therapy; Biological and medical sciences; Biological Transport; Blood and lymphatic vessels; Blood Proteins - chemistry; Blood Proteins - physiology; Blood. Blood and plasma substitutes. Blood products. Blood cells. Blood typing. Plasmapheresis. Apheresis; Cardiology. Vascular system; Cation Transport Proteins - chemistry; Cation Transport Proteins - physiology; Diseases of the peripheral vessels. Diseases of the vena cava. Miscellaneous; Emergency and intensive care: techniques, logistics; Escherichia coli; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - physiology; Gene Expression Regulation; Humans; Intensive care medicine; Intensive care unit. Emergency transport systems. Emergency, hospital ward; Medical sciences; Membrane Glycoproteins - chemistry; Membrane Glycoproteins - physiology; Models, Molecular; Nucleotidyltransferases - physiology; PII Nitrogen Regulatory Proteins - physiology; Protein Conformation; Quaternary Ammonium Compounds - metabolism; Rh-Hr Blood-Group System - chemistry; Rh-Hr Blood-Group System - physiology; Rhesus; Rhésus; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - physiology; Signal Transduction; Species Specificity; Structure-Activity Relationship; Substrate Specificity; Transfusions. Complications. Transfusion reactions. Cell and gene therapy; Transport d'ammonium; Transport d'ammonium; Ammonium transport; Rhesus; Rhésus; AmtB; Escherichia coli; Ammonium; Transfusion; Yeast; Glycoprotein; Mep/Amt; Functional complementation; Rh glycoproteins; Bacteria; Transport; Enterobacteriaceae; Sensor
• ISSN: 1246-7820
• DOI: 10.1016/j.tracli.2006.02.015

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.