[Conversion of zinc finger protein to artificial site-specific nuclease: application to chromosome mapping and sequencing].
Zinc finger motif is a novel DNA binding motif characterized by the unique role of zinc; the protein folding and the DNA binding ability are governed by the coordination of a zinc ion. In C2H2-type zinc finger, two cysteines and two histidines contribute to form a globular domain through zinc coordination. The zinc finger of C2H2-type gives promise of recognition for any DNA sequences because of its recognition mode. A C2H2-type zinc finger protein Sp1 has been converted into artificial site-specific nuclease with an attached Ni-based DNA cleavage unit (Gly-Gly-His). This protein cleaved DNA at a single site near the Sp1 recognition sequence. The zinc finger-based nuclease is applicable to chromosome mapping and sequencing.
Division of Biofunctional Chemistry, Kyoto University.
M
M
Nagaoka
Y
Y
Sugiura
D001483:Base Sequence; D002874:Chromosome Mapping; D004247:DNA / Q000378:metabolism; D004262:DNA Restriction Enzymes; D006801:Humans; D008969:Molecular Sequence Data; D016335:Zinc Fingers
D004247:DNA; D004262:DNA Restriction Enzymes