Non-FokI-based zinc finger nucleases.
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.
Imanishi
Miki
M
Institute for Chemical Research, Kyoto University, Kyoto, Japan.
Negi
Shigeru
S
Sugiura
Yukio
Y
D001665:Binding Sites / Q000235:genetics; D002563:Cerium / Q000378:metabolism; D053837:DNA Cleavage; D004720:Endonucleases / Q000235:genetics / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism; D016335:Zinc Fingers / Q000235:genetics*
D010455:Peptides; D002563:Cerium; D004720:Endonucleases