SAXS Examinations of the Redox-Dependent Formation of a DNA-SOD1 Complex

Int J Mol Sci. 2022 Oct 21;23(20):12673. doi: 10.3390/ijms232012673.

Abstract

Cu/Zn superoxide dismutase (SOD1) plays a key role in the maintenance of cellular reactive oxygen species (ROS) homeostasis as an antioxidant enzyme. We recently found that SOD1 is involved in the regulation of gene expression in response to changes in cellular ROS levels by binding to DNA-specific sequences. Moreover, the SOD1 binding to DNA was observed to be redox-dependent in solutions. Thus, we examined the redox-dependent DNA binding of SOD1 by multiple measurements, including small-angle X-ray scattering (SAXS), indicating the redox-dependent formation of a DNA-SOD1 complex in solutions. The redox-dependent formation of the DNA-SOD1 complex could underlie the SOD1 regulation of gene expression.

Keywords: DNA; HADDOCK docking; SAXS; SOD1; redox-dependent binding.

MeSH terms

  • Antioxidants* / metabolism
  • DNA / metabolism
  • Oxidation-Reduction
  • Reactive Oxygen Species / metabolism
  • Scattering, Small Angle
  • Superoxide Dismutase* / genetics
  • Superoxide Dismutase* / metabolism
  • Superoxide Dismutase-1 / genetics
  • Superoxide Dismutase-1 / metabolism
  • X-Ray Diffraction

Substances

  • Superoxide Dismutase-1
  • Reactive Oxygen Species
  • Antioxidants
  • Superoxide Dismutase
  • DNA