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

doi:10.1016/S0092-8674(00)80155-5

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

Research output: Contribution to journal › Article › peer-review

473 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	811-822
Number of pages	12
Journal	Cell
Volume	86
Issue number	5
DOIs	https://doi.org/10.1016/S0092-8674(00)80155-5
Publication status	Published - 6 Sept 1996
Externally published	Yes

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Sijbers, A. M., De Laat, W. L., Ariza, R. R., Biggerstaff, M., Wei, Y. F., Moggs, J. G., Carter, K. C., Shell, B. K., Evans, E., De Jong, M. C., Rademakers, S., De Rooij, J., Jaspers, N. G. J., Hoeijmakers, J. H. J., & Wood, R. D. (1996). Xeroderma pigmentosum group F caused by a defect in a structure-specific DNA repair endonuclease. Cell, 86(5), 811-822. https://doi.org/10.1016/S0092-8674(00)80155-5

@article{4aeb95069456478080876bc45973518c,

title = "Xeroderma pigmentosum group F caused by a defect in a structure-specific DNA repair endonuclease",

abstract = "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.",

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

note = "Funding Information: Correspondence should be addressed to R. D. W. We thank the members of our laboratories for advice and reagents; A. A. Davies, R. Sowdhamini, W. Vermeulen, and T. Yagi for discussions; and E. C. Friedberg for the Rad1–Rad10 proteins. We thank A. J. van Vuuren, A. de Klein, R. van Os, H. Odijk, and J. de Wit for help with the experiments. This work was supported by the Imperial Cancer Research Fund, the Human Frontiers of Science Programme, the Dutch Scientific Organisation (NWO, Foundation for Chemical Research), and the European Community Human Capital and Mobility Programme. ",

year = "1996",

month = sep,

day = "6",

doi = "10.1016/S0092-8674(00)80155-5",

language = "English",

volume = "86",

pages = "811--822",

journal = "Cell",

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Sijbers, AM, De Laat, WL, Ariza, RR, Biggerstaff, M, Wei, YF, Moggs, JG, Carter, KC, Shell, BK, Evans, E, De Jong, MC, Rademakers, S, De Rooij, J, Jaspers, NGJ, Hoeijmakers, JHJ & Wood, RD 1996, 'Xeroderma pigmentosum group F caused by a defect in a structure-specific DNA repair endonuclease', Cell, vol. 86, no. 5, pp. 811-822. https://doi.org/10.1016/S0092-8674(00)80155-5

TY - JOUR

T1 - Xeroderma pigmentosum group F caused by a defect in a structure-specific DNA repair endonuclease

AU - Sijbers, Anneke M.

AU - De Laat, Wouter L.

AU - Ariza, Rafael R.

AU - Biggerstaff, Maureen

AU - Wei, Ying Fei

AU - Moggs, Jonathan G.

AU - Carter, Kenneth C.

AU - Shell, Brenda K.

AU - Evans, Elizabeth

AU - De Jong, Mariska C.

AU - Rademakers, Suzanne

AU - De Rooij, Johan

AU - Jaspers, Nicolaas G.J.

AU - Hoeijmakers, Jan H.J.

AU - Wood, Richard D.

N1 - Funding Information: Correspondence should be addressed to R. D. W. We thank the members of our laboratories for advice and reagents; A. A. Davies, R. Sowdhamini, W. Vermeulen, and T. Yagi for discussions; and E. C. Friedberg for the Rad1–Rad10 proteins. We thank A. J. van Vuuren, A. de Klein, R. van Os, H. Odijk, and J. de Wit for help with the experiments. This work was supported by the Imperial Cancer Research Fund, the Human Frontiers of Science Programme, the Dutch Scientific Organisation (NWO, Foundation for Chemical Research), and the European Community Human Capital and Mobility Programme.

PY - 1996/9/6

Y1 - 1996/9/6

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/16044373761

U2 - 10.1016/S0092-8674(00)80155-5

DO - 10.1016/S0092-8674(00)80155-5

M3 - Article

C2 - 8797827

AN - SCOPUS:16044373761

SN - 0092-8674

VL - 86

SP - 811

EP - 822

JO - Cell

JF - Cell

IS - 5

ER -

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

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