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

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

doi:10.1016/j.tracli.2006.02.015

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

Strathclyde Institute Of Pharmacy And Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

23 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 contribution	La protéine AmtB de Escherichia coli, un sytème modèle pour la compréhension du transport d'ammonium par AmtB et les protéines Rh
Original language	Multiple languages
Pages (from-to)	97-102
Number of pages	6
Journal	Transfusion clinique et biologique : journal de la Société française de transfusion sanguine
Volume	13
Issue number	1-2
DOIs	https://doi.org/10.1016/j.tracli.2006.02.015
Publication status	Published - 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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10.1016/j.tracli.2006.02.015

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Merrick, M., Javelle, A., Durand, A., Severi, E., Thornton, J., Avent, N. D., Conroy, M. J., & Bullough, P. A. (2006). The Escherichia coli AmtB protein as a model system for understanding ammonium transport by Amt and Rh proteins. Transfusion clinique et biologique : journal de la Société française de transfusion sanguine, 13(1-2), 97-102. https://doi.org/10.1016/j.tracli.2006.02.015

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

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.",

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",

author = "M Merrick and A Javelle and A Durand and E Severi and J Thornton and Avent, {N D} and Conroy, {M J} and Bullough, {P A}",

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Merrick, M, Javelle, A, Durand, A, Severi, E, Thornton, J, Avent, ND, Conroy, MJ & Bullough, PA 2006, 'The Escherichia coli AmtB protein as a model system for understanding ammonium transport by Amt and Rh proteins', Transfusion clinique et biologique : journal de la Société française de transfusion sanguine, vol. 13, no. 1-2, pp. 97-102. https://doi.org/10.1016/j.tracli.2006.02.015

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AU - Merrick, M

AU - Javelle, A

AU - Durand, A

AU - Severi, E

AU - Thornton, J

AU - Avent, N D

AU - Conroy, M J

AU - Bullough, P A

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N2 - 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.

AB - 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.

KW - ammonia

KW - biological transport

KW - blood proteins

KW - cation transport proteins

KW - Escherichia coli proteins

KW - gene expression regulation

KW - humans

KW - membrane glycoproteins

KW - models, molecular

KW - nucleotidyltransferases

KW - PII nitrogen regulatory proteins

KW - protein conformation

KW - quaternary ammonium compounds

KW - Rh-Hr blood-group system

KW - saccharomyces cerevisiae proteins

KW - signal transduction

KW - species specificity

KW - structure-activity relationship

KW - substrate specificity

U2 - 10.1016/j.tracli.2006.02.015

DO - 10.1016/j.tracli.2006.02.015

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SN - 1246-7820

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JO - Transfusion clinique et biologique : journal de la Société française de transfusion sanguine

JF - Transfusion clinique et biologique : journal de la Société française de transfusion sanguine

IS - 1-2

ER -

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

Abstract

Keywords

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