FCCC LOGO Faculty Publications
Matsumoto Y , Kim K
Excision of Deoxyribose Phosphate Residues by DNA-Polymerase- Beta During DNA-Repair
Science. 1995 Aug 4;269(5224) :699-702
PMID: ISI:A1995RM70200037   
Back to previous list
Abstract
Eukaryotic DNA polymerase beta (pol beta) can catalyze DNA synthesis during base excision DNA repair. It is shown here that pol beta also catalyzes release of 5'-terminal deoxyribose phosphate (dRP) residues from incised apurinic-apyrimidinic sites, which are common intermediate products in base excision repair. The catalytic domain for this activity resides within an amino-terminal 8-kilodalton fragment of pol beta, which comprises a distinct structural domain of the enzyme. Magnesium is required for the release of dRP from double-stranded DNA but not from a single-stranded oligonucleotide. Analysis of the released products indicates that the excision reaction occurs by beta-elimination rather than hydrolysis.
Notes
Times Cited: 218 Article RM702 SCIENCE