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Domain 3:

Metabolism

Magnesium Transport and Magnesium Homeostasis

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  • Authors: Krisztina M. Papp-Wallace1, and Michael E. Maguire2
  • Editor: Valley Stewart3
  • VIEW AFFILIATIONS HIDE AFFILIATIONS
    Affiliations: 1: Department of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106-4965; 2: Department of Pharmacology, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106-4965; 3: University of California, Davis, Davis, CA
  • Received 14 February 2008 Accepted 17 April 2008 Published 25 September 2008
  • Address correspondence to Krisztina M. Papp-Wallace kmp12@po.cwru.edu
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  • Abstract:

    This review reviews the properties and regulation of the serovar Typhimurium and transporters that mediate Mg influx: CorA and the Mgt P-type ATPases. In addition, potential Mg regulation of transcription and translation, largely via the PhoPQ two component system, is discussed. CorA proteins are a unique class of transporters and are widespread in the and , with rather distant but functional homologs in eukaryotes. The Mgt transporters are highly homologous to other P-type ATPases but are more closely related to the eukaryotic H and Ca ATPases than to most prokaryotic ATPases. Hundreds of homologs of CorA are currently known from genomic sequencing. In contrast, only when extracellular and possibly intracellular Mg levels fall significantly is the expression of and induced. Topology studies using and fusions initially indicated that the serovar Typhimurium CorA contained three transmembrane (TM) segments; however, subsequent data obtained using a variety of approaches showed that the CorA superfamily of proteins have only two TMs at the extreme C terminus. PhoP-PhoQ is a two-component system consisting of PhoQ, the sensor/receptor histidine kinase, and PhoP, the response regulator/transcriptional activator. The expression of both and in either or serovar Typhimurium is markedly induced in a PhoPQ-dependent manner by low concentrations of Mg in the medium. and form an operon with two promoters in both and serovar Typhimurium.

  • Citation: Papp-Wallace K, Maguire M. 2008. Magnesium Transport and Magnesium Homeostasis, EcoSal Plus 2008; doi:10.1128/ecosalplus.5.4.4.2

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2008-09-25
2018-06-23

Abstract:

This review reviews the properties and regulation of the serovar Typhimurium and transporters that mediate Mg influx: CorA and the Mgt P-type ATPases. In addition, potential Mg regulation of transcription and translation, largely via the PhoPQ two component system, is discussed. CorA proteins are a unique class of transporters and are widespread in the and , with rather distant but functional homologs in eukaryotes. The Mgt transporters are highly homologous to other P-type ATPases but are more closely related to the eukaryotic H and Ca ATPases than to most prokaryotic ATPases. Hundreds of homologs of CorA are currently known from genomic sequencing. In contrast, only when extracellular and possibly intracellular Mg levels fall significantly is the expression of and induced. Topology studies using and fusions initially indicated that the serovar Typhimurium CorA contained three transmembrane (TM) segments; however, subsequent data obtained using a variety of approaches showed that the CorA superfamily of proteins have only two TMs at the extreme C terminus. PhoP-PhoQ is a two-component system consisting of PhoQ, the sensor/receptor histidine kinase, and PhoP, the response regulator/transcriptional activator. The expression of both and in either or serovar Typhimurium is markedly induced in a PhoPQ-dependent manner by low concentrations of Mg in the medium. and form an operon with two promoters in both and serovar Typhimurium.

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Magnesium Transport and Magnesium Homeostasis
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Citation: Papp-Wallace K, Maguire M. 2008. Magnesium Transport and Magnesium Homeostasis, EcoSal Plus 2008; doi:10.1128/ecosalplus.5.4.4.2
/content/ecosalplus/10.1128/ecosalplus.5.4.4.2.fig1a
Figure 1A

The protein is oriented with the periplasm at the top. The blue arrows denoting the β-sheets show the orientation of each strand with the arrow pointing from N terminus to C terminus.

ecosalplus/3/1/5.4.4.2_fig_001_thmb.gif
ecosalplus/3/1/5.4.4.2_fig_001.gif
Image of Figure 1A
Figure 1A

The protein is oriented with the periplasm at the top. The blue arrows denoting the β-sheets show the orientation of each strand with the arrow pointing from N terminus to C terminus.

Citation: Papp-Wallace K, Maguire M. 2008. Magnesium Transport and Magnesium Homeostasis, EcoSal Plus 2008; doi:10.1128/ecosalplus.5.4.4.2
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Figure 1B

ecosalplus/3/1/5.4.4.2_fig_002_thmb.gif
ecosalplus/3/1/5.4.4.2_fig_002.gif
Image of Figure 1B
Figure 1B

Citation: Papp-Wallace K, Maguire M. 2008. Magnesium Transport and Magnesium Homeostasis, EcoSal Plus 2008; doi:10.1128/ecosalplus.5.4.4.2
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Figure 1C

Note that TM1 (light green) and TM2 (magenta) are not connected. The 9-aa sequence that connects the two TM segments is not resolved in any of the current crystal structures available (see the text).

ecosalplus/3/1/5.4.4.2_fig_003_thmb.gif
ecosalplus/3/1/5.4.4.2_fig_003.gif
Image of Figure 1C
Figure 1C

Note that TM1 (light green) and TM2 (magenta) are not connected. The 9-aa sequence that connects the two TM segments is not resolved in any of the current crystal structures available (see the text).

Citation: Papp-Wallace K, Maguire M. 2008. Magnesium Transport and Magnesium Homeostasis, EcoSal Plus 2008; doi:10.1128/ecosalplus.5.4.4.2
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Tables

Magnesium Transport and Magnesium Homeostasis
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Citation: Papp-Wallace K, Maguire M. 2008. Magnesium Transport and Magnesium Homeostasis, EcoSal Plus 2008; doi:10.1128/ecosalplus.5.4.4.2
/content/ecosalplus/10.1128/ecosalplus.5.4.4.2.T1
Table 1

Properties of ions of common biological cations

Generic image for table
Table 1

Properties of ions of common biological cations

Citation: Papp-Wallace K, Maguire M. 2008. Magnesium Transport and Magnesium Homeostasis, EcoSal Plus 2008; doi:10.1128/ecosalplus.5.4.4.2

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