Accession Number:

ADA210751

Title:

Synthetic sequence Specific Nucleases

Descriptive Note:

Annual rept. 1 Aug 1988-15 Jul 1989

Corporate Author:

CALIFORNIA UNIV LOS ANGELES

Personal Author(s):

• Sigman, David S.

Report Date:

1989-07-15

Pagination or Media Count:

13.0

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.

Descriptors:

• *PEPTIDES
• *MOLECULAR BIOLOGY
• *NUCLEASE
• SITES
• SEQUENCES
• CHEMICAL REACTIONS
• CUTTING
• PROTEINS
• COILS
• CONTROL
• DEOXYRIBONUCLEIC ACIDS

Subject Categories:

• Biochemistry
• Genetic Engineering and Molecular Biology

Distribution Statement:

APPROVED FOR PUBLIC RELEASE