Structural Insights into Iron Ions Accumulation in Dps Nanocage

Int J Mol Sci. 2022 May 10;23(10):5313. doi: 10.3390/ijms23105313.

Abstract

Dps (DNA-binding protein from starved cells) is well known for the structural protection of bacterial DNA by the formation of highly ordered intracellular assemblies under stress conditions. Moreover, this ferritin-like protein can perform fast oxidation of ferrous ions and subsequently accumulate clusters of ferric ions in its nanocages, thus providing the bacterium with physical and chemical protection. Here, cryo-electron microscopy was used to study the accumulation of iron ions in the nanocage of a Dps protein from Escherichia coli. We demonstrate that Fe2+ concentration in the solution and incubation time have an insignificant effect on the volume and the morphology of iron minerals formed in Dps nanocages. However, an increase in the Fe2+ level leads to an increase in the proportion of larger clusters and the clusters themselves are composed of discrete ~1-1.5 nm subunits.

Keywords: DNA-binding protein from starved cells (Dps); Fe minerals; cryo-electron microscopy; iron nanoparticles; mini-ferritin; single particle analysis.

MeSH terms

  • Bacterial Outer Membrane Proteins / genetics
  • Cryoelectron Microscopy
  • Escherichia coli / metabolism
  • Escherichia coli Proteins* / genetics
  • Ferritins* / metabolism
  • Ions / metabolism
  • Iron / metabolism

Substances

  • Bacterial Outer Membrane Proteins
  • Escherichia coli Proteins
  • Ions
  • dps protein, E coli
  • Ferritins
  • Iron