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Science 13 January 1995:
Vol. 267. no. 5195, pp. 237 - 240
DOI: 10.1126/science.7809628
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Articles

Science, Vol 267, Issue 5195, 237-240
Copyright © 1995 by American Association for the Advancement of Science

articles

Cleavage of an amide bond by a ribozyme

X Dai, A De Mesmaeker, and GF Joyce

Department of Chemistry, Scripps Research Institute, La Jolla, CA 92037.

A variant form of a group I ribozyme, optimized by in vitro evolution for its ability to catalyze magnesium-dependent phosphoester transfer reactions involving DNA substrates, also catalyzes the cleavage of an unactivated alkyl amide when that linkage is presented in the context of an oligodeoxynucleotide analog. Substrates containing an amide bond that joins either two DNA oligos, or a DNA oligo and a short peptide, are cleaved in a magnesium-dependent fashion to generate the expected products. The first-order rate constant, kcat, is 0.1 x 10(-5) min-1 to 1 x 10(-5) min-1 for the DNA-flanked substrates, which corresponds to a rate acceleration of more than 10(3) as compared with the uncatalyzed reaction.


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Specific, rapid synthesis of Phe-RNA by RNA.
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Versatile 5' phosphoryl coupling of small and large molecules to an RNA.
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