Natural and artificial zinc finger proteins
نویسنده
چکیده
Zinc finger proteins acquire DNA-binding ability by Zn (II) complexation. In the zinc finger domain of the Cys2His2 type, each finger is approximately 30 amino acid residues long and consists of a simple ββα–fold stabilized by chelation of a zinc ion with the conserved Cys2His2 residues. A zinc finger motif of Cys2His2 offers an attractive framework for the design of a novel DNA-binding protein. Multiple-zinc-finger peptides have been generated from the three-zinc-finger motif of transcription factor Spl. The nine-zinc-finger peptide showed 27-base-pair DNA binding. A DNA-bending finger was also designed to regulate gene expression. By connecting two DNA-binding domains of Sp1 through a flexible polyglycine linker, new bending finger peptides were created. In addition, an artificial DNA cutter was engineered by combining a zinc finger protein with a glycylglycylhistidine site. Such novel zinc finger peptides provide great potential for use as genome-specific transcription switches in the near future.
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