Isolation of active recombinant XPG protein, a human DNA repair endonuclease.

@article{ODonovan1994IsolationOA,
  title={Isolation of active recombinant XPG protein, a human DNA repair endonuclease.},
  author={Anne O'Donovan and Daniel Scherly and Stuart G. Clarkson and Richard D Wood},
  journal={The Journal of biological chemistry},
  year={1994},
  volume={269 23},
  pages={15965-8}
}
Complementation group G of xeroderma pigmentosum (XP-G) is one of the most rare and phenotypically heterogeneous forms of this inherited disorder. XP-G patients vary from having a very mild defect in DNA repair to being severely affected, and a few cases are also associated with the neurological complications of Cockayne's syndrome. The XPG gene encodes an acidic protein with a predicted molecular mass of 133 kDa that confers normal UV resistance when expressed in XP-G cells. Here we report the… CONTINUE READING