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Chimeric restriction endonuclease.
Open accessAbstract
Fok I restriction endonuclease recognizes the nonpalindromic pentadeoxyribonucleotide 5'-GGATG-3'.5'-CATCC-3' in duplex DNA and cleaves 9 and 13 nt away from the recognition site. Recently, we reported the presence of two distinct and separable domains within this enzyme: one for the sequence-specific recognition of DNA (the DNA-binding domain) and the other for the endonuclease activity (the cleavage domain). Here, we report the construction of a chimeric restriction endonuclease by linking the Drosophila Ultrabithorax homeodomain to the cleavage domain (FN) of Fok I restriction endonuclease. The hybrid enzyme, Ubx-FN, was purified, and its cleavage properties were characterized. The hybrid enzyme shows the same DNA sequence-binding preference as that of Ubx; as expected, it cleaves the DNA away from the recognition site. On the 5'-TTAATGGTT-3' strand the hybrid enzyme cleaves 3 nt away from the recognition site, whereas it cuts the complementary 5'-AACCATTAA-3' strand 8, 9, or 10 nt away from the binding site. Similarly engineered hybrid enzymes could be valuable tools in physical mapping and sequencing of large eukaryotic genomes.
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Citations
Cited by
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
Self-citationGenome Engineering With Zinc-Finger Nucleases
Carroll, D. (2011) · Genetics · doi:10.1534/genetics.111.131433 · Cited by 1,076
Gene targeting using zinc finger nucleases
Porteus, M. H., & Carroll, D. (2005) · Nature Biotechnology · doi:10.1038/nbt1125 · Cited by 641
Genome Engineering with Targetable Nucleases
Carroll, D. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060713-035418 · Cited by 568
Durai, S. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki912 · Cited by 522
Metadata
- Authors
- Kim, Y. G., & Chandrasegaran, S.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1994-02
- Volume
- 91
- Issue
- 3
- Pages
- 883-887
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2075529916
- Cited by
- 189
- References
- 0
- FWCI
- 1.35
- Type
- journal article
- Language
- en
- Open access
- green
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