The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Human DNA Repair Excision Nuclease
Open accessAbstract
Human DNA repair excision nuclease removes DNA damage by incising on both sides of the lesion in a precise manner. The activity requires participation of 16-17 polypeptides. Of these, the XPF.ERCC1 complex and XPG were predicted to carry the nuclease active sites based on studies with the recombinant proteins and the yeast homologs of these proteins. Furthermore, recent work with model (undamaged) substrates have led to predictions of the roles of these proteins in incising 5' or 3' to the lesion. We have used damaged DNA substrates and antibodies to XPG and ERCC1 to test these predictions. Our results reveal that anti-XPG antibodies change the site of 3' incision and at high concentration inhibit the 3' incision without significantly affecting the 5' incision, indicating that XPG makes the 3' incision and further that under this condition 5' incision can occur without 3' incision. In contrast, anti-ERCC1 antibodies inhibit both the 3' and 5' incisions. Using a defined system for excision repair we also demonstrate that the 3' incision can occur without the 5' incision, leading us to conclude that under certain conditions the two incisions can occur independently.
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Citations
Cites
Reconstitution of Human DNA Repair Excision Nuclease in a Highly Defined System
Mu, D., Park, C.-H., Matsunaga, T., Hsu, D. S., Reardon, J. T., & Sancar, A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.6.2415 · Cited by 476
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Cited by
Molecular mechanism of nucleotide excision repair
de Laat, W. L., Jaspers, N. G. J., & Hoeijmakers, J. H. J. (1999) · Genes & Development · doi:10.1101/gad.13.7.768 · Cited by 1,122
Molecular Mechanisms of Mammalian Global Genome Nucleotide Excision Repair
Gillet, L. C. J., & Schärer, O. D. (2006) · Chemical Reviews · doi:10.1021/cr040483f · Cited by 642
A multistep damage recognition mechanism for global genomic nucleotide excision repair
Sugasawa, K., Okamoto, T., Shimizu, Y., Masutani, C., Iwai, S., & Hanaoka, F. (2001) · Genes & Development · doi:10.1101/gad.866301 · Cited by 435
Chemistry and Biology of DNA Repair
Schärer, O. D. (2003) · Angewandte Chemie International Edition · doi:10.1002/anie.200200523 · Cited by 381
Reardon, J. T., Bessho, T., Kung, H. C., Bolton, P. H., & Sancar, A. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.17.9463 · Cited by 366
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Metadata
- Authors
- Matsunaga, T., Mu, D., Park, C.-H., Reardon, J. T., & Sancar, A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-09
- Volume
- 270
- Issue
- 35
- Pages
- 20862-20869
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1975853177
- Cited by
- 216
- References
- 1
- FWCI
- 6.63
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Matsunaga, T., Mu, D., Park, C.-H., Reardon, J. T., & Sancar, A. (1995). Human DNA Repair Excision Nuclease. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.270.35.20862
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
