The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
Fok I dimerization is required for DNA cleavage
Open accessAbstract
Fok I is a type IIs restriction endonuclease comprised of a DNA recognition domain and a catalytic domain. The structural similarity of the Fok I catalytic domain to the type II restriction endonuclease Bam HI monomer suggested that the Fok I catalytic domains may dimerize. In addition, the Fok I structure, presented in an accompanying paper in this issue of Proceedings , reveals a dimerization interface between catalytic domains. We provide evidence here that Fok I catalytic domain must dimerize for DNA cleavage to occur. First, we show that the rate of DNA cleavage catalyzed by various concentrations of Fok I are not directly proportional to the protein concentration, suggesting a cooperative effect for DNA cleavage. Second, we constructed a Fok I variant, Fok N13Y, which is unable to bind the Fok I recognition sequence but when mixed with wild-type Fok I increases the rate of DNA cleavage. Additionally, the Fok I catalytic domain that lacks the DNA binding domain was shown to increase the rate of wild-type Fok I cleavage of DNA. We also constructed an Fok I variant, Fok D483A, R487A, which should be defective for dimerization because the altered residues reside at the putative dimerization interface. Consistent with the Fok I dimerization model, the variant Fok D483A, R487A revealed greatly impaired DNA cleavage. Based on our work and previous reports, we discuss a pathway of DNA binding, dimerization, and cleavage by Fok I endonuclease.
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Cites
Hybrid restriction enzymes: zinc finger fusions to Fok I cleavage domain.
Kim, Y. G., Cha, J., & Chandrasegaran, S. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.3.1156 · Cited by 1,889
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Structure of Bam HI Endonuclease Bound to DNA: Partial Folding and Unfolding on DNA Binding
Newman, M., Strzelecka, T., Dorner, L. F., Schildkraut, I., & Aggarwal, A. K. (1995) · Science · doi:10.1126/science.7624794 · Cited by 298
Self-citationStructure of the multimodular endonuclease FokI bound to DNA
Wah, D. A., Hirsch, J. A., Dorner, L. F., Schildkraut, I., & Aggarwal, A. K. (1997) · Nature · doi:10.1038/40446 · Cited by 266
Self-citationProtein Splicing Involving the Saccharomyces cerevisiae VMA Intein
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Structure of Fok I has implications for DNA cleavage
Wah, D. A., Bitinaite, J., Schildkraut, I., & Aggarwal, A. K. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.18.10564 · Cited by 202
Self-citationStructure and function of restriction endonucleases
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Self-citationChimeric restriction endonuclease.
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Structure of restriction endonuclease BamHI and its relationship to EcoRI
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New restriction endonucleases from Flavobacterium okeanokoites (FokI) and Micrococcus luteus (MluI)
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Tebas, P., Stein, D., Tang, W. W., Frank, I., Wang, S. Q., Lee, G., Spratt, S. K., Surosky, R. T., Giedlin, M. A., Nichol, G., et al. (2014) · New England Journal of Medicine · doi:10.1056/nejmoa1300662 · Cited by 1,357
Richardson, C. D., Ray, G. J., DeWitt, M. A., Curie, G. L., & Corn, J. E. (2016) · Nature Biotechnology · doi:10.1038/nbt.3481 · Cited by 1,098
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Metadata
- Authors
- Bitinaite, J., Wah, D. A., Aggarwal, A. K., & Schildkraut, I.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1998-09
- Volume
- 95
- Issue
- 18
- Pages
- 10570-10575
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2126237980
- Cited by
- 490
- References
- 21
- FWCI
- 2.81
- Type
- journal article
- Language
- en
- Open access
- green
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