Synthetic sequence Specific Nucleases
Abstract
The principal goal of this research was to determine if synthetic peptides derived from the helix-turn-helix domain binding proteins can be converted into a site specific nuclease by linking it to the nuclease of 1,10- phenanthroline-copper. In this work, we have shown that a synthetic peptide derived from the helix-turn-helix binding domain of the E. Coli trp repressor can be converted into a chemical nuclease activity targeted for the aro H operator which is regulated by this control protein. The cutting by the peptide is not as specific as that observed by the chemically derivatized parent protein. Preferred scission is observed because DNA stabilizes the random coil protein in a helix-turn-helix conformation on its surface.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 15, 1989
- Accession Number
- ADA210751
Entities
People
- David S. Sigman
Organizations
- University of California, Los Angeles