Abstract
Catalysts have been generated that sequence-specifically hydrolyze RNA and DNA at predefined sites, i.e., a new class of restriction enzymes. New binding domains (oligonucleotides or peptides of defined sequence) were introduced site-selectively into the relatively nonselective phosphodiesterases, staphylococcal nuclease and ribonuclease S, to generate hybrid enzymes that site-specifically cleave nucleic acids. Subsequent mutagenesis of the hybrid enzymes has generated enzymes that siteselectively hydrolyze one bond in large RNAs and DNAs in a catalytic fashion. We have been able to use these hybrid enzymes to selectively cleave duplex plasmid DNAs via D-loop formation. This work has not only resulted in powerful tools for studying RNA and DNA structure but also may provide a general strategy for designing other selective hybrid enzymes for important biological transformations, such as the selective cleavage of genomic DNA, or selective cleavage of peptide amide bonds.
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Zuckermann R, Schultz PG, Raines RT, Rutter WJ. Manuscript in preparation
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Corey, D.R., Zuckermann, R.N., Schultz, P.G. (1991). Hybrid Enzymes and the Sequence-Specific Cleavage of Nucleic Acids. In: Dugas, H. (eds) Bioorganic Chemistry Frontiers. Bioorganic Chemistry Frontiers, vol 2. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76241-3_1
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DOI: https://doi.org/10.1007/978-3-642-76241-3_1
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