Xeroderma pigmentosum group F caused by a defect in a structure-specific DNA repair endonuclease

Anneke M. Sijbers, Wouter L. De Laat, Rafael R. Ariza, Maureen Biggerstaff, Ying Fei Wei, Jonathan G. Moggs, Kenneth C. Carter, Brenda K. Shell, Elizabeth Evans, Mariska C. De Jong, Suzanne Rademakers, Johan De Rooij, Nicolaas G.J. Jaspers, Jan H.J. Hoeijmakers, Richard D. Wood

Onderzoeksoutput: Bijdrage aan tijdschriftArtikelpeer review

455 Citaten (Scopus)

Samenvatting

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-specific endonuclease responsible for the 5' incision during repair. These results demonstrate that the XPF, ERCC4, and ERCC11 genes are equivalent, complete the isolation of the XP genes that form the core nucleotide excision repair system, and solve the catalytic function of the XPF-containing complex.

Originele taal-2Engels
Pagina's (van-tot)811-822
Aantal pagina's12
TijdschriftCell
Volume86
Nummer van het tijdschrift5
DOI's
StatusGepubliceerd - 6 sep. 1996
Extern gepubliceerdJa

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