EXCISION OF DEOXYRIBOSE PHOSPHATE RESIDUES BY DNA-POLYMERASE-BETA DURING DNA-REPAIR
EXCISION OF DEOXYRIBOSE PHOSPHATE RESIDUES BY DNA-POLYMERASE-BETA DURING DNA-REPAIR
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DOI:
10.1126/science.7624801
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发表时间:
1995-08-04
期刊:
影响因子:
56.9
通讯作者:
KIM, K
中科院分区:
文献类型:
--
作者:
MATSUMOTO, Y;KIM, K
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.