Structure-Based Design of Transcription Factors
Copyright policy )Structure-Based Design of Transcription Factors
Computer modeling suggested that transcription factors with novel sequence specificities could be designed by combining known DNA binding domains. This structure-based strategy was tested by construction of a fusion protein, ZFHD1, that contained zinc fingers 1 and 2 from Zif268, a short polypeptide linker, and the homeodomain from Oct-1. The fusion protein bound optimally to a sequence containing adjacent homeodomain (TAATTA) and zinc finger (NGGGNG) subsites. When fused to an activation domain, ZFHD1 regulated promoter activity in vivo in a sequence-specific manner. Analysis of known protein-DNA complexes suggests that many other DNA binding proteins could be designed in a similar fashion.
- Center for Cancer Research United States
- National Cancer Institute United States
- Massachusetts Institute of Technology United States
- Harvard–MIT Division of Health Sciences and Technology United States
Homeodomain Proteins, Models, Molecular, Binding Sites, Base Sequence, Recombinant Fusion Proteins, Molecular Sequence Data, Zinc Fingers, Protein Engineering, Transfection, DNA-Binding Proteins, Gene Expression Regulation, Computer Simulation, Amino Acid Sequence, Cloning, Molecular, Promoter Regions, Genetic, Host Cell Factor C1, Octamer Transcription Factor-1, Transcription Factors
Homeodomain Proteins, Models, Molecular, Binding Sites, Base Sequence, Recombinant Fusion Proteins, Molecular Sequence Data, Zinc Fingers, Protein Engineering, Transfection, DNA-Binding Proteins, Gene Expression Regulation, Computer Simulation, Amino Acid Sequence, Cloning, Molecular, Promoter Regions, Genetic, Host Cell Factor C1, Octamer Transcription Factor-1, Transcription Factors
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