XPG endonuclease makes the 3' incision in human DNA nucleotide excision repair - PubMed (original) (raw)
. 1994 Sep 29;371(6496):432-5.
doi: 10.1038/371432a0.
Affiliations
- PMID: 8090225
- DOI: 10.1038/371432a0
XPG endonuclease makes the 3' incision in human DNA nucleotide excision repair
A O'Donovan et al. Nature. 1994.
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.
Comment in
- DNA repair. Incisions for excision.
Hoeijmakers JH, Bootsma D. Hoeijmakers JH, et al. Nature. 1994 Oct 20;371(6499):654-5. doi: 10.1038/371654a0. Nature. 1994. PMID: 7935809 No abstract available.
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