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

被引:23
|
作者
Merrick, M
Javelle, A
Durand, A
Severi, E
Thornton, J
Avent, ND
Conroy, MJ
Bullough, PA
机构
[1] John Innes Ctr, Dept Mol Microbiol, Norwich NR4 7UH, Norfolk, England
[2] Univ W England, Ctr Biomed Res, Bristol BS16 1QY, Avon, England
[3] Univ Sheffield, Dept Mol Biol & Biotechnol, Krebs Inst Biomol Res, Western Bank, Sheffield S10 2ITN, S Yorkshire, England
基金
英国生物技术与生命科学研究理事会;
关键词
ammonium transports; Escherichia coli; AmtB; rhesus;
D O I
10.1016/j.tracli.2006.02.015
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
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 Arnt proteins and genetic approaches are also now being used to dissect structure/function relationships in Arnt proteins. The now well-recognised homology between the Arnt proteins, found in archaca, eubacteria, fungi and plants, and the Rhesus proteins, found characteristically in animals, also means that studies on I-E. coli AmtB can potentially shed light oil structure/ function relationships in the clinically important Rh proteins. (c) 2006 Elsevier SAS. All rights reserved.
引用
收藏
页码:97 / 102
页数:6
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