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={Anneke M. Sijbers and Wouter de Laat and Rafael R Ariza and Maureen Biggerstaff and Ying-Fei Wei and Jonathan Moggs and K C Carter and Brenda K. Shell and Elizabeth Evans and Mariska C. 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}
}

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References

SHOWING 1-10 OF 117 REFERENCES
Isolation of active recombinant XPG protein, a human DNA repair endonuclease.
TLDR
This work reports the isolation of full-length XPG as a soluble protein expressed from a recombinant baculovirus and reports the first direct evidence for a human protein with properties that implicate it in the incision step of nucleotide excision repair.
Clinical heterogeneity within xeroderma pigmentosum associated with mutations in the DNA repair and transcription gene ERCC3.
TLDR
Two new XP-B patients are identified by microneedle injection of the cloned ERCC3 repair gene as well as by cell hybridization, revealing a single base substitution causing a missense mutation in a region that is completely conserved in yeast, Drosophila, mouse, and human ER CC3.
Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23.
TLDR
The purification to homogeneity and subsequent cDNA cloning of a repair complex by in vitro complementation of the XP‐C defect in a cell‐free repair system containing UV‐damaged SV40 minichromosomes implies that the complex exerts a unique function in the genome‐overall repair pathway which is important for prevention of skin cancer.
Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA.
TLDR
The results suggest that XPAC functions as a key component in recognition of DNA damage during repair, and is involved in an early step of nucleotide excision repair, the main process that removes UV damage and many chemical lesions from DNA.
Evidence for a repair enzyme complex involving ERCC1 and complementing activities of ERCC4, ERCC11 and xeroderma pigmentosum group F.
TLDR
Complementation analysis in vitro of rodent CGs is accomplished by pairwise mixing of mutant extracts, and results show that mutants from groups 2, 3, 5 and XP‐A can complement all other CGs tested, however, selective non‐complementation in vitro was observed in mutual mixtures of groups 1, 4, 11 andXP‐F, suggesting that the complementing activities involved somehow affect each other.
XPG endonuclease makes the 3′ incision in human DNA nucleotide excision repair
TLDR
It is shown that XPG makes a structure-specific endonucleolytic incision in a synthetic DNA substrate containing a duplex region and single-stranded arms, by cleaving 3' to DNA damage during nucleotide excision repair.
Co‐correction of the ERCC1, ERCC4 and xeroderma pigmentosum group F DNA repair defects in vitro.
TLDR
It is reported that repair of UV‐irradiated DNA can be reconstituted by combining rodent group 1 cell extracts with correcting protein from HeLa cells and the data suggest that ERCC1 is part of a functional protein complex with group 4 and XP‐F correcting activities.
ERCC4 (XPF) encodes a human nucleotide excision repair protein with eukaryotic recombination homologs
TLDR
The ERCC4 gene structure and functional cDNA sequence encoding a 916-amino-acid protein has substantial homology with the eukaryotic DNA repair and recombination proteins MEI-9, Rad16, and Rad1 (Saccharomyces cerevisiae).
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