Design of novel zinc finger proteins: towards artificial control of specific gene expression.
In this review, we summarize design strategies for generating proteins with desired sequences such as long contiguous base pairs and diverse sequence specificities based on the nature of Cys(2)-His(2) zinc finger proteins. Recent progress towards artificial DNA binding proteins has been achieved by structure-based design processes and by selection strategies. Indeed, a multi-zinc finger protein with an 18 (or 27)-base pair address, and new zinc finger proteins for diverse DNA target sites (TATA-box and p53 binding site) have been created successfully. Such novel zinc finger proteins will probably be useful tools in molecular biology and potentially in human medicine.
Imanishi
M
M
Institute for Chemical Research, Kyoto University, Uji, 611-0011, Kyoto, Japan.
Hori
Y
Y
Nagaoka
M
M
Sugiura
Y
Y
D000818:Animals; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D051766:Early Growth Response Protein 1; D015870:Gene Expression / Q000502:physiology*; D016158:Genes, p53 / Q000502:physiology; D006801:Humans; D017874:Immediate-Early Proteins; D016385:TATA Box / Q000502:physiology; D014157:Transcription Factors / Q000737:chemistry / Q000378:metabolism*; D015533:Transcriptional Activation / Q000187:drug effects / Q000502:physiology*
D004268:DNA-Binding Proteins; C497325:EGR1 protein, human; D051766:Early Growth Response Protein 1; D017874:Immediate-Early Proteins; D014157:Transcription Factors; D004247:DNA