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SUMOylation of XRCC1 activated by poly (ADP-ribosyl)ation regulates DNA repair

Ling-Yueh Hu1, Che-Chang Chang2, Yen-Sung Huang1

  • 1Institute of Biomedical Sciences, Academia Sinica, Taipei 115, Taiwan.

Human Molecular Genetics
|April 19, 2018
PubMed

Insights

DNA damage triggers poly(ADP-ribosyl)ation (PARylation) of XRCC1, enhancing its SUMOylation. This modification recruits DNA polymerase beta (POLB), promoting efficient base excision repair (BER) and genomic stability.

Area of Science:

  • Molecular Biology
  • Genomics
  • DNA Repair Mechanisms

Background:

  • XRCC1 is a crucial scaffold protein for base excision repair (BER), vital for maintaining genomic stability.
  • While XRCC1 is a known substrate for SUMOylation, the regulation and functional impact of this modification on BER remain unclear.

Purpose of the Study:

  • To elucidate the regulatory mechanisms of XRCC1 SUMOylation under DNA damaging conditions.
  • To investigate the role of SUMOylated XRCC1 in the base excision repair pathway.

Main Methods:

  • Methyl methanesulfonate (MMS) treatment to induce DNA damage.
  • Analysis of XRCC1 SUMOylation and its interaction with PARP1 and TOPORS.
  • Assessment of DNA polymerase beta (POLB) binding and DNA repair capacity using a SUMOylation-defective XRCC1 mutant.

Main Results:

  • MMS treatment induces XRCC1 SUMOylation, which facilitates BER.
  • Poly(ADP-ribose) polymerase 1 (PARP1) activation by MMS leads to poly(ADP-ribose) (PAR) synthesis, promoting TOPORS recruitment and XRCC1 SUMOylation.
  • A SUMOylation-defective XRCC1 mutant exhibited reduced POLB binding and impaired repair of MMS-induced DNA damage.

Conclusions:

  • DNA damage-induced PARylation promotes XRCC1 SUMOylation.
  • SUMOylated XRCC1 enhances POLB recruitment, leading to more efficient BER.
  • This pathway is critical for maintaining genomic stability following DNA damage.

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