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Non-canonical interaction of DNA repair proteins with intact and cleaved AP sites

Svetlana Khodyreva1, Olga Lavrik2

  • 1Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, 630090, Novosibirsk, Russia.

DNA Repair
|June 4, 2020
PubMed

Insights

This review explores novel proteins interacting with DNA's apurinic/apyrimidinic (AP) sites. These interactions, forming Schiff bases, suggest backup DNA repair pathways, crucial for genomic stability.

Area of Science:

  • Genomic stability and DNA repair mechanisms.
  • Biochemistry of DNA lesions and protein interactions.

Background:

  • Apurinic/apyrimidinic (AP) sites are common, mutagenic DNA lesions from various sources.
  • Efficient repair of AP sites is essential for preventing mutations.

Purpose of the Study:

  • To identify previously unrecognized proteins that interact with intact or cleaved AP sites.
  • To investigate proteins forming Schiff bases upon interaction with AP sites.

Main Methods:

  • Literature review focusing on proteins interacting with AP sites.
  • Analysis of Schiff base formation between proteins and AP site aldehydes.

Main Results:

  • Several proteins capable of interacting with AP sites, forming Schiff bases, have been identified.
  • These interactions lead to AP site processing, albeit less efficiently than canonical AP/dRP lyases.

Conclusions:

  • The identified protein interactions may represent backup pathways for DNA repair.
  • Understanding these interactions is vital for comprehending the full scope of DNA repair processes.
Keywords:
ABH1AP siteApe1Base excision repairDNA-protein cross-linkDeoxyribose phosphateGAPDHHMGAHMGB1Ku antigenPARP

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