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Related Experiment Videos

Magnesium transport in prokaryotes.

M B Moncrief1, M E Maguire

  • 1Department of Pharmacology, School of Medicine Case Western Reserve University, 10900 Euclid Avenue Cleveland, OH 44106-4965, USA.

Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry
|November 7, 1999
PubMed
Summary

Magnesium (Mg2+) transport into cells involves unique systems like CorA, MgtE, MgtA, and MgtB. These transporters exhibit diverse structures and regulatory mechanisms, crucial for cellular magnesium homeostasis and bacterial virulence.

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The CorA Mg(2+) transport protein of Salmonella typhimurium. Mutagenesis of conserved residues in the second membrane domain.

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The CorA Mg2+ transport protein of Salmonella typhimurium. Mutagenesis of conserved residues in the third membrane domain identifies a Mg2+ pore.

The Journal of biological chemistry·1998

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Microbiology

Background:

  • Magnesium ion (Mg2+) transport across cell membranes presents a unique challenge due to its physicochemical properties.
  • Salmonella typhimurium serves as a model organism for studying Mg2+ transporters due to its well-established genetic tools.
  • Several Mg2+ transport systems, including CorA, MgtE, MgtA, and MgtB, have been identified in bacteria.

Purpose of the Study:

  • To elucidate the characteristics and mechanisms of various Mg2+ transport systems in bacteria.
  • To investigate the genetic regulation and functional roles of Mg2+ transporters, particularly in Salmonella typhimurium.
  • To understand the structural and functional diversity of proteins involved in cellular magnesium uptake.

Main Methods:

  • Genetic characterization and cloning of Mg2+ transporter genes in Salmonella typhimurium.

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  • Sequence homology analysis to identify related transport proteins and potential functions.
  • Investigation of gene regulation by two-component systems, such as PhoP/PhoQ, under varying Mg2+ conditions.

    • Main Results:

    • CorA is a constitutively expressed, major Mg2+ transporter in Eubacteria and Archaea, with a unique domain structure.
    • MgtA and MgtB are homologous to P-type ATPases and mediate Mg2+ influx along the electrochemical gradient, regulated by PhoP/PhoQ.
    • MgtC, part of the mgtCB operon, is essential for virulence and appears to function as a Mg2+ transporter, despite lacking homology to known proteins.

    Conclusions:

    • Bacterial Mg2+ transporters display significant diversity in structure, mechanism, and regulation.
    • The PhoP/PhoQ system plays a critical role in regulating Mg2+ transport under nutrient-limiting conditions.
    • Mg2+ transport systems are unique and employ unusual mechanisms for mediating ion movement across membranes, with implications for bacterial physiology and pathogenesis.