The design of functional proteins is one of the most challenging areas of protein research. We have constructed zinc finger peptides with metal-dependent hydrolytic abilities by mutating the zinc ligands in classical zinc fingers, without the need to add a FokI or other DNA cleavage domain. The designed peptides acquired DNA cleavage ability successfully, retaining the proper zinc finger folding and DNA targeting ability. We have also succeeded in site-specific DNA cleavage in the presence of cerium ions by introducing a lanthanide ion-binding loop as a linker of zinc finger motifs. © 2010 Springer Science+Business Media, LLC.
CITATION STYLE
Imanishi, M., Negi, S., & Sugiura, Y. (2010). Non-FokI-based zinc finger nucleases. Methods in Molecular Biology, 649, 337–349. https://doi.org/10.1007/978-1-60761-753-2_21
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