DNA polymerase β-dependent long patch base excision repair in living cells

Kenjiro Asagoshi, Yuan Liu, Aya Masaoka, Li Lan, Rajendra Prasad, Julie K. Horton, Ashley R. Brown, Xiao hong Wang, Hussam M. Bdour, Robert W. Sobol, John Stephen Taylor, Akira Yasui, Samuel H. Wilson

Research output: Contribution to journalArticlepeer-review

44 Citations (Scopus)


We examined a role for DNA polymerase β (Pol β) in mammalian long patch base excision repair (LP BER). Although a role for Pol β is well known in single-nucleotide BER, information on this enzyme in the context of LP BER has been limited. To examine the question of Pol β involvement in LP BER, we made use of nucleotide excision repair-deficient human XPA cells expressing UVDE (XPA-UVDE), which introduces a nick directly 5′ to the cyclobutane pyrimidine dimer or 6-4 photoproduct, leaving ends with 3′-OH and 5′-phosphorylated UV lesion. We observed recruitment of GFP-fused Pol β to focal sites of nuclear UV irradiation, consistent with a role of Pol β in repair of UV-induced photoproducts adjacent to a strand break. This was the first evidence of Pol β recruitment in LP BER in vivo. In cell extract, a 5′-blocked oligodeoxynucleotide substrate containing a nicked 5′-cyclobutane pyrimidine dimer was repaired by Pol β-dependent LP BER. We also demonstrated Pol β involvement in LP BER by making use of mouse cells that are double null for XPA and Pol β. These results were extended by experiments with oligodeoxynucleotide substrates and purified human Pol β.

Original languageEnglish
Pages (from-to)109-119
Number of pages11
JournalDNA Repair
Issue number2
Publication statusPublished - 2010 Feb 4
Externally publishedYes


  • DNA polymerase β
  • Flap endonuclease 1
  • Long patch base excision repair
  • Thymine dimer
  • UV damage endonuclease

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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