Xeroderma Pigmentosum Group F Caused by a Defect in a Structure-Specific DNA Repair Endonuclease

@article{Sijbers1996XerodermaPG,
  title={Xeroderma Pigmentosum Group F Caused by a Defect in a Structure-Specific DNA Repair Endonuclease},
  author={A. M. Sijbers and Wouter de Laat and Rafael R Ariza and Maureen Biggerstaff and Ying-fei Wei and Jonathan G. Moggs and Kenneth C. Carter and Brenda K Shell and Elizabeth Evans and M. D. de Jong and Suzanne Rademakers and Johan de Rooij and Nicolaas G. J. Jaspers and Jan H. J. Hoeijmakers and Richard D Wood},
  journal={Cell},
  year={1996},
  volume={86},
  pages={811-822}
}
Nucleotide excision repair, which is defective in xeroderma pigmentosum (XP), involves incision of a DNA strand on each side of a lesion. We isolated a human gene homologous to yeast Rad1 and found that it corrects the repair defects of XP group F as well as rodent groups 4 and 11. Causative mutations and strongly reduced levels of encoded protein were identified in XP-F patients. The XPF protein was purified from mammalian cells in a tight complex with ERCC1. This complex is a structure… CONTINUE READING