Role of polymerase β in complementing aprataxin deficiency during abasic-site base excision repair

Nat Struct Mol Biol. 2014 May;21(5):497-9. doi: 10.1038/nsmb.2818. Epub 2014 Apr 28.


DNA polymerase β (pol β) lyase removal of 5'-deoxyribose phosphate (5'-dRP) from base excision repair (BER) intermediates is critical in mammalian BER involving the abasic site. We found that pol β also removes 5'-adenylated dRP from BER intermediates after abortive ligation. The crystal structure of a human pol β-DNA complex showed the 5'-AMP-dRP group positioned in the lyase active site. Pol β expression rescued methyl methanesulfonate sensitivity in aprataxin (hnt3)- and FEN1 (rad27)-deficient yeast.

Publication types

  • Research Support, N.I.H., Intramural

MeSH terms

  • Crystallography, X-Ray
  • DNA / chemistry
  • DNA Polymerase beta / chemistry*
  • DNA Polymerase beta / physiology
  • DNA Repair*
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism
  • DNA-Binding Proteins / physiology
  • Humans
  • Models, Molecular
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / metabolism
  • Nuclear Proteins / physiology
  • Protein Structure, Tertiary


  • APTX protein, human
  • DNA-Binding Proteins
  • Nuclear Proteins
  • DNA
  • DNA Polymerase beta

Associated data

  • PDB/4O9M