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Structure of Fok I has implications for DNA cleavage
Open accessAbstract
Fok I is a member an unusual class of restriction enzymes that recognize a specific DNA sequence and cleave nonspecifically a short distance away from that sequence. Fok I consists of an N-terminal DNA recognition domain and a C-terminal cleavage domain. The bipartite nature of Fok I has led to the development of artificial enzymes with novel specificities. We have solved the structure of Fok I to 2.3 Å resolution. The structure reveals a dimer, in which the dimerization interface is mediated by the cleavage domain. Each monomer has an overall conformation similar to that found in the Fok I–DNA complex, with the cleavage domain packing alongside the DNA recognition domain. In corroboration with the cleavage data presented in the accompanying paper in this issue of Proceedings , we propose a model for Fok I DNA cleavage that requires the dimerization of Fok I on DNA to cleave both DNA strands.
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Cited by
An improved zinc-finger nuclease architecture for highly specific genome editing
Miller, J. C., Holmes, M. C., Wang, J., Guschin, D. Y., Lee, Y.-L., Rupniewski, I., Beausejour, C. M., Waite, A. J., Wang, N. S., Kim, K. A., et al. (2007) · Nature Biotechnology · doi:10.1038/nbt1319 · Cited by 1,051
Durai, S. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki912 · Cited by 522
Structure-based redesign of the dimerization interface reduces the toxicity of zinc-finger nucleases
Szczepek, M., Brondani, V., Büchel, J., Serrano, L., Segal, D. J., & Cathomen, T. (2007) · Nature Biotechnology · doi:10.1038/nbt1317 · Cited by 501
Fok I dimerization is required for DNA cleavage
Bitinaite, J., Wah, D. A., Aggarwal, A. K., & Schildkraut, I. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10570 · Cited by 490
Self-citationEnhancing zinc-finger-nuclease activity with improved obligate heterodimeric architectures
Doyon, Y., Vo, T. D., Mendel, M. C., Greenberg, S. G., Wang, J., Xia, D. F., Miller, J. C., Urnov, F. D., Gregory, P. D., & Holmes, M. C. (2011) · Nature Methods · doi:10.1038/nmeth.1539 · Cited by 402
Metadata
- Authors
- Wah, D. A., Bitinaite, J., Schildkraut, I., & Aggarwal, A. K.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1998-09
- Volume
- 95
- Issue
- 18
- Pages
- 10564-10569
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2118514248
- Cited by
- 202
- References
- 0
- FWCI
- 2.81
- Type
- journal article
- Language
- en
- Open access
- green
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- Wah, D. A., Bitinaite, J., Schildkraut, I., & Aggarwal, A. K. (1998). Structure of Fok I has implications for DNA cleavage. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.95.18.10564
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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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