Letter abstract
Nature Chemical Biology 3, 763 - 768 (2007)
Published online: 28 October 2007 | doi:10.1038/nchembio.2007.45
Dissecting metal ion–dependent folding and catalysis of a single DNAzyme
Hee-Kyung Kim1, Ivan Rasnik2,4, Juewen Liu1, Taekjip Ha2,3 & Yi Lu1
Protein metalloenzymes use various modes for functions for which metal-dependent global conformational change is required in some cases but not in others. In contrast, most ribozymes require a global folding that almost always precedes enzyme reactions. Herein we studied metal-dependent folding and cleavage activity of the 8–17 DNAzyme using single-molecule fluorescence resonance energy transfer. Addition of Zn2+ and Mg2+ induced folding of the DNAzyme into a more compact structure followed by a cleavage reaction, which suggests that the DNAzyme may require metal-dependent global folding for activation. In the presence of Pb2+, however, the cleavage reaction occurred without a precedent folding step, which suggests that the DNAzyme may be prearranged to accept Pb2+ for the activity. Neither ligation reaction of the cleaved substrates nor dynamic changes between folded and unfolded states was observed. These features may contribute to the unusually fast Pb2+-dependent reaction of the DNAzyme. These results suggest that DNAzymes can use all modes of activation that metalloproteins use.
- Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Mathews Avenue, Urbana, Illinois 61801, USA.
- Department of Physics, University of Illinois at Urbana-Champaign, 1110 West Green Street, Urbana, Illinois 61801-3080, USA.
- Howard Hughes Medical Institute, 1110 West Green Street, Urbana, Illinois 61801, USA.
- Present address: Emory University, Department of Physics, 400 Dowman Drive, Atlanta, Georgia 30322-2430, USA.
Correspondence to: Taekjip Ha2,3 e-mail: tjha@uiuc.edu
Correspondence to: Yi Lu1 e-mail: yi-lu@uiuc.edu
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