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The role of UV-DDB in processing 8-oxoguanine during base excision repair

Ashna Nagpal1,2, Sripriya Raja1,2, Bennett Van Houten1,2

  • 1UPMC Hillman Cancer Center, University of Pittsburgh, Pittsburgh, PA 15213, U.S.A.

Biochemical Society Transactions
|October 28, 2022
PubMed

Insights

The UV-damaged DNA-binding protein (UV-DDB) facilitates DNA repair by stimulating key enzymes like OGG1 and APE1. It also helps BER enzymes access damaged DNA within chromatin.

Area of Science:

  • Molecular Biology
  • DNA Repair Mechanisms
  • Biochemistry

Background:

  • Nucleotide excision repair (NER) proteins UV-damaged DNA-binding protein (UV-DDB), xeroderma pigmentosum group C (XPC), and xeroderma pigmentosum group A (XPA) are implicated in 8-oxoG processing.
  • 8-oxoG is a common oxidative DNA lesion requiring efficient repair pathways.

Approach:

  • Biochemical studies demonstrating UV-DDB's stimulation of human 8-oxoG glycosylase (OGG1), MUTYH, and AP endonuclease (APE1).
  • Single-molecule studies showing UV-DDB association with repair proteins at abasic sites.
  • Cell experiments investigating UV-DDB interactions with OGG1 at 8-oxoG sites.
  • Development of a model for UV-DDB's role in chromatin remodeling for base excision repair (BER).

Key Points:

  • UV-DDB enhances the activity of OGG1, MUTYH, and APE1 at DNA damage sites.
  • UV-DDB physically interacts with OGG1 at 8-oxoG lesions in cellular contexts.
  • UV-DDB may act as an initial factor to modify nucleosome structure, enabling BER enzyme access to damaged DNA.
  • This highlights a novel role for UV-DDB beyond NER in oxidative DNA damage processing.

Conclusions:

  • UV-DDB plays a crucial role in facilitating the repair of oxidative DNA damage, particularly 8-oxoG.
  • The protein's ability to stimulate glycosylases and remodel chromatin suggests a central function in coordinating DNA repair.
  • Further research into UV-DDB's mechanisms can inform therapeutic strategies for diseases associated with DNA damage accumulation.
Keywords:
8-oxoguanineOGG1UV-DDBbase excision repairnucleotide excision repair

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