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XB-ART-19383
Science 1995 Aug 04;2695224:699-702. doi: 10.1126/science.7624801.
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Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair.

Matsumoto Y , Kim K .


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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.

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Species referenced: Xenopus laevis
Genes referenced: utrn