Base flipping free energy profiles for damaged and undamaged DNA

Chem Res Toxicol. 2010 Dec 20;23(12):1868-70. doi: 10.1021/tx1003613.

Abstract

Lesion-induced thermodynamic destabilization is believed to facilitate β-hairpin intrusion by the human XPC/hHR23B nucleotide excision repair (NER) recognition factor, accompanied by partner-base flipping, as suggested by the crystal structure of the yeast orthologue (Min, J. H., and Pavletich, N. P. (2007) Nature 449, 570-575). To investigate this proposed mechanism, we employed the umbrella sampling method to compute partner base flipping free energies for the repair susceptible 14R (+)-trans-anti-DB[a,l]P-N(2)-dG modified duplex 11-mer, derived from the fjord region polycyclic aromatic hydrocarbon dibenzo[a,l]pyrene, and for the undamaged duplex. Our flipping free energy profiles show that the adduct has a lower flipping barrier by ∼7.7 kcal/mol, consistent with its thermally destabilizing impact on the damaged DNA duplex and its susceptibility to NER.

Publication types

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

MeSH terms

  • Benzopyrenes / chemistry
  • DNA / chemistry*
  • DNA / metabolism
  • DNA Adducts / chemistry
  • DNA Damage*
  • DNA Repair
  • DNA Repair Enzymes / metabolism
  • DNA-Binding Proteins / metabolism
  • Humans
  • Molecular Dynamics Simulation
  • Thermodynamics

Substances

  • Benzopyrenes
  • DNA Adducts
  • DNA-Binding Proteins
  • RAD23B protein, human
  • XPC protein, human
  • dibenzo(a,i)pyrene
  • DNA
  • DNA Repair Enzymes