Abstract
We have isolated a large number of polynucleotide kinase ribozymes from a pool of RNA molecules consisting of an ATP-binding domain flanked by regions of random sequence. Different classes of kinases catalyse the transfer of the γ-thiophosphate of ATP-γS to the 5′-hydroxyl or to internal 2′-hydroxyls. An engineered version of one class is able to catalyse the transfer of thiophosphate from ATP-γS to the 5′-hydroxyl of an exogenous oligoribonucleotide substrate with multiple turnover, thus acting as a true enzyme.
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Lorsch, J., Szostak, J. In vitro evolution of new ribozymes with polynucleotide kinase activity. Nature 371, 31–36 (1994). https://doi.org/10.1038/371031a0
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DOI: https://doi.org/10.1038/371031a0
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