Structure-based redesign of the dimerization interface reduces the toxicity of zinc-finger nucleases

@article{Szczepek2007StructurebasedRO,
  title={Structure-based redesign of the dimerization interface reduces the toxicity of zinc-finger nucleases},
  author={Michal Szczepek and Vincent Brondani and Janine B{\"u}chel and L. Durb{\'a}n Serrano and David J Segal and Toni Cathomen},
  journal={Nature Biotechnology},
  year={2007},
  volume={25},
  pages={786-793}
}
Artificial endonucleases consisting of a FokI cleavage domain tethered to engineered zinc-finger DNA-binding proteins have proven useful for stimulating homologous recombination in a variety of cell types. Because the catalytic domain of zinc-finger nucleases (ZFNs) must dimerize to become active, two subunits are typically assembled as heterodimers at the cleavage site. The use of ZFNs is often associated with significant cytotoxicity, presumably due to cleavage at off-target sites. Here we… CONTINUE READING
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