Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 130, Issue 40, Pages 13194-13195Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja804653f
Keywords
-
Categories
Funding
- U.S. Department of Energy, Division of Materials Sciences [DE-FG03-00ER46051]
- Skaggs Institute for Chemical Biology
Ask authors/readers for more resources
An E. coli catabolite activator protein (CAP) has been converted into a sequence-specific DNA cleaving protein by genetically introducing (2,2'-bipyridin-5-yl)alanine (Bpy-Ala) into the protein. The mutant CAP (CAP-K26Bpy-Ala) showed comparable binding affinity to CAP-WT for the consensus operator sequence. In the presence of Cu(II) and 3-mercaptopropionic acid, CAP-K26Bpy-Ala cleaves double-stranded DNA with high sequence specificity. This method should provide a useful tool for mapping the molecular details of protein-nucleic acid interactions.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available