2014, Vol.10(6), p.e1004429
Magnesium is an essential divalent metal that serves many cellular functions. While most divalent cations are maintained at relatively low intracellular concentrations, magnesium is maintained at a higher level (∼0.5–2.0 mM). Three families of transport proteins were previously identified for magnesium import: CorA, MgtE, and MgtA/MgtB P-type ATPases. In the current study, we find that expression of a bacterial protein unrelated to these transporters can fully restore growth to a bacterial mutant that lacks known magnesium transporters, suggesting it is a new importer for magnesium. We demonstrate that this transport activity is likely to be specific rather than resulting from substrate promiscuity because the proteins are incapable of manganese import. This magnesium transport protein is distantly related to the Nramp family of proteins, which have been shown to transport divalent cations but have never been shown to recognize magnesium. We also find gene expression of the new magnesium transporter to be controlled by a magnesium-sensing riboswitch. Importantly, we find additional examples of riboswitch-regulated homologues, suggesting that they are a frequent occurrence in bacteria. Therefore, our aggregate data discover a new and perhaps broadly important path for magnesium import and highlight how identification of riboswitch RNAs can help shed light on new, and sometimes unexpected, functions of their downstream genes. ; Magnesium ions are essential for life, and, correspondingly, all organisms must encode for proteins to transport them. Three classes of bacterial proteins (CorA, MgtE and MgtA/B) have previously been identified for transport of the ion. This current study introduces a new route of magnesium import, which, moreover, is unexpectedly provided by proteins distantly related to Natural esistance-ssociated acrophage roteins (Nramp). Nramp metal transporters are widespread in the three domains of life; however, most are assumed to function as transporters of transition metals such as manganese or iron. None of the previously characterized Nramps have been shown to transport magnesium. In this study, we demonstrate that certain bacterial proteins, distantly related to Nramp homologues, exhibit transport of magnesium. We also find that these new magnesium transporters are genetically controlled by a magnesium-sensing regulatory element. Importantly, we find numerous additional examples of similar genes sharing this regulatory arrangement, suggesting that these genes may be a frequent occurrence in bacteria, and may represent a class of magnesium transporters. Therefore, our aggregate data discover a new and perhaps broadly important path of magnesium import in bacteria.
Research Article ; Biology And Life Sciences ; Research And Analysis Methods