Merrick M, Javelle A, Durand A, Severi E, Thornton J, Avent N D, Conroy M J, Bullough P A
Department of Molecular Microbiology, John Innes Centre, Colney Lane, Norwich, NR4 7UH Norwich, UK.
Transfus Clin Biol. 2006 Mar-Apr;13(1-2):97-102. doi: 10.1016/j.tracli.2006.02.015. Epub 2006 Mar 24.
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.
大肠杆菌铵转运蛋白(AmtB)已成为用于分析普遍存在的内膜蛋白Amt家族铵摄取过程的首选模型系统。在过去6年中,我们在该系统中开发了一系列遗传和生化工具。这些工具使结构/功能分析得以迅速发展,最初提供了对该蛋白膜拓扑结构的深入了解,最近则促成了高分辨率三维结构的解析。遗传分析揭示了一种新的调控机制,该机制在原核Amt蛋白中显然是保守的,并且遗传方法现在也被用于剖析Amt蛋白中的结构/功能关系。古细菌、真细菌、真菌和植物中发现的Amt蛋白与动物中特有的恒河猴蛋白之间现已得到充分认可的同源性,也意味着对大肠杆菌AmtB的研究可能有助于阐明临床上重要的Rh蛋白的结构/功能关系。