The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Functional and Physical Interaction between WRN Helicase and Human Replication Protein A
Open accessAbstract
The human premature aging disorder Werner syndrome (WS) is associated with a large number of symptoms displayed in normal aging. The WRN gene product, a DNA helicase, has been previously shown to unwind short DNA duplexes (</=53 base pairs) in a reaction stimulated by single-stranded DNA-binding proteins. We have studied the helicase activity of purified WRN protein on a variety of DNA duplex substrates to characterize the unwinding properties of the enzyme in greater detail. WRN helicase can catalyze unwinding of long duplex DNA substrates up to 849 base pairs in a reaction dependent on human replication protein A (hRPA). Escherichia coli SSB and bacteriophage T4 gene 32 protein (gp32) completely failed to stimulate WRN helicase to unwind long DNA duplexes indicating a specific functional interaction between WRN and hRPA. So far, there have been no reports of any physical interactions between WRN helicase and other proteins. In support of the functional interaction, we demonstrate a direct interaction between WRN and hRPA by coimmunoprecipitation of purified proteins. The physical and functional interaction between WRN and hRPA suggests that the two proteins may function together in vivo in a pathway of DNA metabolism such as replication, recombination, or repair.
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Positional Cloning of the Werner's Syndrome Gene
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The Bloom's syndrome gene product is homologous to RecQ helicases
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Mammalian 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
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ESCHERICHIA COLI SINGLE-STRANDED DNA-BINDING PROTEIN: Multiple DNA-Binding Modes and Cooperativities
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The Werner syndrome protein is a DNA helicase
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Cited by
Human RecQ Helicases in DNA Repair, Recombination, and Replication
Croteau, D. L., Popuri, V., Opresko, P. L., & Bohr, V. A. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060713-035428 · Cited by 538
Self-citationMaréchal, A., & Zou, L. (2015) · Cell Research · doi:10.1038/cr.2014.147 · Cited by 465
Fabre, F., Chan, A., Heyer, W.-D., & Gangloff, S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.252652399 · Cited by 323
Johnson, F. B., Marciniak, R. A., McVey, M., Stewart, S. A., Hahn, W. C., & Guarente, L. (2001) · The EMBO Journal · doi:10.1093/emboj/20.4.905 · Cited by 269
Brosh, Jr. (2001) · The EMBO Journal · doi:10.1093/emboj/20.20.5791 · Cited by 260
Metadata
- Authors
- Brosh, R. M., Orren, D. K., Nehlin, J. O., Ravn, P. H., Kenny, M. K., Machwe, A., & Bohr, V. A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-06
- Volume
- 274
- Issue
- 26
- Pages
- 18341-18350
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2059501883
- Cited by
- 306
- References
- 48
- FWCI
- 7.61
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Brosh, R. M., Orren, D. K., Nehlin, J. O., Ravn, P. H., Kenny, M. K., Machwe, A., & Bohr, V. A. (1999). Functional and Physical Interaction between WRN Helicase and Human Replication Protein A. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.274.26.18341
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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