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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   
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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.
Times Cited: 218 Article RM702 SCIENCE