The Small Protein MntS and Exporter MntP Optimize the Intracellular Concentration of Manganese

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The model organism Escherichia coli can employ manganese to activate a variety of enzymes, but it does so only when iron is unavailable or the cell is assaulted by oxidants. Under those stress conditions, E. coli activates the synthesis of its MntH manganese importer. However, manganese can also be toxic, and over-accumulation of the metal must be avoided. We investigated additional mechanisms by which the cell ensures that its intracellular manganese pool is sufficient but not excessive. MntS was identified as a small protein that is synthesized when manganese levels decline; it helps to enlarge the manganese pool. In contrast, MntP is a manganese exporter that is synthesized when intracellular manganese levels rise; it keeps manganese levels from becoming too high. In manganese-rich medium either the forced expression of MntS or the absence of MntP led to manganese toxicity, suggesting the possibility that MntS operates as an inhibitor of MntP. This toxicity occurs because excess manganese inhibits the synthesis of heme, a cofactor that is essential for aerobic growth. Thus E. coli controls manganese levels by balancing the actions of MntH, MntP, and MntS against one another. This arrangement allows cells to adapt to shifts in manganese availability and demand.

Vyšlo v časopise: The Small Protein MntS and Exporter MntP Optimize the Intracellular Concentration of Manganese. PLoS Genet 11(3): e32767. doi:10.1371/journal.pgen.1004977
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pgen.1004977

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