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"XPG endonuclease makes the 3' incision in human DNA nucleotide excision repair." |
O'Donovan A, Davies AA, Moggs JG, West SC, Wood RD |
Published Sept. 1, 1994 in Nature volume 371 .
Pubmed ID: 8090225
Abstract:
| Humans with a defect in the XPG protein suffer from xeroderma pigmentosum (XP) resulting from an inability to perform DNA nucleotide excision repair properly. Here we show that XPG makes a structure-specific endonucleolytic incision in a synthetic DNA substrate containing a duplex region and single-stranded arms. One strand of the duplex is cleaved at the border with single-stranded DNA. A cut with the same polarity is also made in a bubble structure, at the 3' side of the centrally unpaired region. Normal cell extracts introduce a nick 3' to a platinum-DNA lesion, but an XP-G cell extract is defective in making this incision. These data show that XPG has a direct role in making one of the incisions required to excise a damaged oligonucleotide, by cleaving 3' to DNA damage during nucleotide excision repair. |
This publication refers to following REPAIRtoire entries:
| Genes | |
| Proteins |
Last modification of this entry: Oct. 6, 2010
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