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Determination of recognition sites of T4 RNA ligase on the 3′-OH and 5′-P termini of polyribonucleotide chains

Abstract

RNA LIGASE which was discovered by Silber et al.1 in T4-infected Escherichia coli cells, catalyses an ATP-dependent, intramolecular joining reacion of 5′-P and 3′-OH termini of various homopolyribonucleotides1,2. The shortest circularising polyadenylate was shown to be (pA)8, the optimal chain length for the reaction being 10–30 (ref. 2). These facts suggest that the substrate for T4 RNA ligase is a pair of suitably juxtaposed, 3′-OH and 5′-P termini, each a few single stranded residues long2.

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References

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    Kasai, K., and Grunberg-Manago, M., Eur. J. Biochem., 1, 152–167 (1967).

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