Fokl restriction endonuclease

Fig. 5. Schematic of the construction and function of chimeric restriction endonucleases (Chandrasegaran and Smith, 1999). (a) The type IIS restriction enzyme Fokl has a nonspecific endonuclease domain (FN) and a DNA-binding domain. Swapping Fokl s DNA binding-domain for that of another DNA binding-domain results in a chimeric restriction enzyme with new specificity. The flexibility resulting from less intimate contact between the Fn domain and its new DNA-binding domain translates into DNA cleavage at several locations near the binding site, (b) The modular nature and tunable specificity of zinc...

Fokl A type IIS restriction endonuclease derived from Flavobacterium okeanokoites... 

R. A. and Matthews, B.W., Type II restriction endonucleases structural, functional, and evolutionary relationships, Curr. Opin. Chem. Biol. 3, 578-583, 1999 Akar, A., Orkunoglu, F.E., Ozata, M., Sengul, A., and Gur, A.R., Lack of association between vitamin D receptor Fokl polymorphism and alopecia areata, Eur. J. Dermatol. 14, 156-158, 2004 Guy, M., Lowe, L.C., Bretherton-Watt, D. et al., Vitamin D receptor gene polymorphisms and breast cancer risk, Clin. Cancer Res. 10, 5472-5481, 2004 Claassen, M., Nouwen, J., Fang, Y. et al., Staphylococcus aureus nasal carriage is not associated with known polymorphism in the Vitamin D receptor gene, FEMS Immunol. Med. Microbiol. 43,173-176, 2005 Bolu,... 

Of the type IIS restriction endonucleases that have been reasonably well characterized, e.g., Fokl, FIgal, Hphl, and Mboll, the Fokl R-M enzymes from Flavobac-terium okeanokoites are probably the best studied, which is the reason for the focus of this section. Fokl R and M enzymes specifically recognize the sequence 5 -GGATG-373 -CCTAC-5. R-Fokl (66 kDa) cleaves the DNA at a site 9 and 13 nucleotides to the right of the top and bottom recognition sequences. 

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