XPG endonuclease makes the 3' incision in human DNA nucleotide excision repair.
作者： Anne O'Donovan , Adelina A. Davies , Jonathan G. Moggs , Stephen C. West , Richard D. Wood
DOI: 10.1038/371432A0
关键词:
摘要: HUMANS with a defect in the XPG protein suffer from xeroderma pigmentosum (XP) resulting an inability to perform DNA nucleotide excision repair properly1–4. Here we show that makes structure-specific endonucleolytic incision synthetic substrate containing duplex region and single-stranded arms. One strand of is cleaved at border DNA. A cut same polarity also made bubble structure, 3′ side centrally unpaired region. Normal cell extracts introduce nick platinum – lesion, but XP-G extract defective making this incision. These data has direct role one incisions required excise damaged oligonucleotide, by cleaving 3' damage during repair.
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