A fresh view of the cell biology of copper in enterobacteria

Mol Microbiol. 2013 Feb;87(3):447-54. doi: 10.1111/mmi.12123. Epub 2012 Dec 17.


Copper ions are essential but also very toxic. Copper resistance in bacteria is based on export of the toxic ion, oxidation from Cu(I) to Cu(II), and sequestration by copper-binding metal chaperones, which deliver copper ions to efflux systems or metal-binding sites of copper-requiring proteins. In their publication in this issue, Osman et al. (2013) demonstrate how tightly copper resistance, homeostasis and delivery pathways are interwoven in Salmonella enterica sv. Typhimurium. Copper is transported from the cytoplasm by the two P-type ATPases CopA and GolT to the periplasm and transferred to SodCII by CueP, a periplasmic copper chaperone. When copper levels are higher, SodCII is also able to bind copper without the help of CueP. This scheme raises the question as to why copper ions present in the growth medium have to make the detour through the cytoplasm. The data presented in the publication by Osman et al. (2013) change our view of the cell biology of copper in enterobacteria.

Publication types

  • Research Support, Non-U.S. Gov't
  • Comment

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Bacterial Proteins / metabolism*
  • Carrier Proteins / metabolism*
  • Copper / metabolism*
  • Membrane Transport Proteins / metabolism*
  • Salmonella typhimurium / enzymology*
  • Salmonella typhimurium / metabolism*
  • Superoxide Dismutase / metabolism*


  • Bacterial Proteins
  • Carrier Proteins
  • CopA protein, Bacteria
  • Membrane Transport Proteins
  • copper-binding protein
  • Copper
  • Superoxide Dismutase
  • Adenosine Triphosphatases