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Cellular accumulation of Cys326-OGG1 protein complexes under conditions of oxidative stress

M P Kaur1, E J Guggenheim1, C Pulisciano1

  • 1School of Biosciences, The University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom.

Biochemical and Biophysical Research Communications
|April 1, 2014
PubMed

Insights

The Ser326Cys variant of 8-oxoguanine glycosylase 1 (OGG1) forms redox-sensitive protein complexes under oxidative stress. This accumulation may explain the reduced DNA repair capacity linked to this common polymorphism.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • The Ser326Cys polymorphism in 8-oxoguanine glycosylase 1 (OGG1) is linked to reduced oxidative DNA repair capacity.
  • Individuals with Cys326-OGG1 homozygous genotype may have increased susceptibility to certain cancers.
  • Previous studies suggest OGG1 redox modification and dimer formation contribute to reduced repair capacity.

Purpose of the Study:

  • To visualize the accumulation of Cys326-OGG1 protein complexes in living cells using bimolecular fluorescence complementation.
  • To investigate the role of oxidative stress in the formation of OGG1 protein complexes.

Main Methods:

  • Bimolecular fluorescence complementation (BiFC) was employed to study OGG1 protein complex formation in situ.
  • Cellular oxidative stress was induced by depleting glutathione levels using buthionine sulfoximine.
  • The effect of thiol reducing agents (β-mercaptoethanol, dithiothreitol) and an antioxidant (dimethyl sulfoxide) on OGG1 complex formation was assessed.

Main Results:

  • Specific fluorescence indicating Cys326-OGG1 complex formation was observed within and around the nucleus of cells under oxidative stress.
  • Complex formation was dependent on the presence of Cys326-OGG1 and induced by glutathione depletion.
  • OGG1 complex formation was inhibited by reducing agents and an antioxidant, confirming the role of oxidative stress.

Conclusions:

  • This study provides the first direct evidence of redox-sensitive Cys326-OGG1 protein accumulation in cells experiencing intracellular oxidative stress.
  • The observed OGG1 complex formation under oxidative stress conditions may underlie the reduced DNA repair capacity associated with the Cys326-OGG1 polymorphism.
Keywords:
BiFC visualisationDimerOGG1Oxidative stress

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