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

Gabriel Kaufmann, Neville R. Kallenbach

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)452-454
Number of pages3
JournalNature
Volume254
Issue number5499
DOIs
StatePublished - 1975

ASJC Scopus subject areas

  • General

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