In molecular biology, BpuJI is a type II restriction endonuclease which recognises the asymmetricsequence 5'-CCCGT and cuts at multiple sites in the surrounding area of the target sequence. The BpuJI protein consists of two distinct modules; an N-terminal DNA recognition domain, and a C-terminal dimerisation and catalysis domain. The N-terminal domain is composed of two winged-helix subdomains and a disrupted linker subdomain. Target sequence recognition occurs through major groove contacts of amino acids in the winged-helix subdomains.[1]
References
^Sukackaite R, Grazulis S, Bochtler M, Siksnys V (May 2008). "The recognition domain of the BpuJI restriction endonuclease in complex with cognate DNA at 1.3-A resolution". J. Mol. Biol. 378 (5): 1084â-93. doi:10.1016/j.jmb.2008.03.041. PMID18433771.
