Restriction enzyme FokI(Internal) Rabbit Polyclonal Antibody

Function

The enzyme FokI, naturally found in Flavobacterium okeanokoites, is a bacterial type IIS restriction endonuclease consisting of an N-terminal DNA-binding domain and a non-specific DNA cleavage domain at the C-terminal. Once the protein is bound to duplex DNA via its DNA-binding domain at the 5'-GGATG-3':3'-CATCC-5' recognition site, the DNA cleavage domain is activated and cleaves, without further sequence specificity, the first strand 9 nucleotides downstream and the second strand 13 nucleotides upstream of the nearest nucleotide of the recognition site. Its molecular mass is 65.4 kDa, being composed of 587 amino acids.

Background References

1. Bitinaite, J.; D. A. Wah, Aggarwal, A. K., Schildkraut, I. (1998). "FokI dimerization is required for DNA cleavage". Proc Natl Acad Sci USA 95 (18): 10570-5.

2. Strandberg, S.; et al. (2003). "Vitamin D receptor start codon polymorphism (FokI) is related to bone mineral density in healthy adolescent boys". J Bone Miner Metab. 21 (2): 109-13.

3. Durai S, Mani M, Kandavelou K, Wu J, Porteus M, Chandrasegaran S (2005). "Zinc finger nucleases: custom-designed molecular scissors for genome engineering of plant and mammalian cells". Nucleic Acids Res 33 (18): 5978-90.

UNIPROT

SwissProt: P14870 Planomicrobium okeanokoites