期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 130, 期 40, 页码 13194-13195出版社
AMER CHEMICAL SOC
DOI: 10.1021/ja804653f
关键词
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资金
- U.S. Department of Energy, Division of Materials Sciences [DE-FG03-00ER46051]
- Skaggs Institute for Chemical Biology
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.
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