The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Replication Protein A Confers Structure-specific Endonuclease Activities to the XPF-ERCC1 and XPG Subunits of Human DNA Repair Excision Nuclease
Open accessAbstract
XPF-ERCC1 and XPG proteins are nucleases that are involved in human nucleotide excision repair. In this study, we characterized the structure-specific junction-cutting activities of both nucleases using DNA substrates containing a bubble or loop structure. We found that the junction-cutting activities of XPF-ERCC1 and XPG were greatly stimulated by human replication protein A (RPA), while heterologous single-stranded DNA-binding proteins could not substitute for human RPA. To test for specific interaction between RPA and XPF-ERCC1 as is known to occur between RPA and XPG, we employed a pull-down assay with immobilized "bubble" substrate. We found that the binding of XPF-ERCC1 complex to the bubble substrate was enhanced by RPA, suggesting a possible mechanism for RPA in the excision nuclease system, that is the targeting of the nuclease subunits to their specific sites of action. Furthermore, the RPA-promoted junction cutting by XPF-ERCC1 and XPG nucleases was observed with "loop" substrates as well, raising the possibility that XPF-ERCC1, XPG, and RPA may function in removing loop structures from DNA, independent of the other subunits of the human excinuclease.
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Cites
Sancar, A. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.000355 · Cited by 1,131
Self-citationMammalian DNA nucleotide excision repair reconstituted with purified protein components
Aboussekhra, A., Biggerstaff, M., Shivji, M. K. K., Vilpo, J. A., Moncollin, V., Podust, V. N., Protić, M., Hübscher, U., Egly, J.-M., & Wood, R. D. (1995) · Cell · doi:10.1016/0092-8674(95)90289-9 · Cited by 837
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
Self-citationRPA involvement in the damage-recognition and incision steps of nucleotide excision repair
He, Z., Henricksen, L. A., Wold, M. S., & Ingles, C. J. (1995) · Nature · doi:10.1038/374566a0 · Cited by 389
Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA
Jones, C. J., & Wood, R. D. (1993) · Biochemistry · doi:10.1021/bi00096a021 · Cited by 291
Cited by
Wold, M. S. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.61 · Cited by 1,444
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
Molecular Interaction Map of the Mammalian Cell Cycle Control and DNA Repair Systems
Kohn, K. W. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.8.2703 · Cited by 560
Maréchal, A., & Zou, L. (2015) · Cell Research · doi:10.1038/cr.2014.147 · Cited by 465
Metadata
- Authors
- Matsunaga, T., Park, C.-H., Bessho, T., Mu, D., & Sancar, A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1996-05
- Volume
- 271
- Issue
- 19
- Pages
- 11047-11050
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2062028908
- Cited by
- 190
- References
- 5
- FWCI
- 6.93
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Matsunaga, T., Park, C.-H., Bessho, T., Mu, D., & Sancar, A. (1996). Replication Protein A Confers Structure-specific Endonuclease Activities to the XPF-ERCC1 and XPG Subunits of Human DNA Repair Excision Nuclease. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.271.19.11047
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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