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

Gabriel Kaufmann; Neville R. Kallenbach

doi:10.1038/254452a0

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

Gabriel Kaufmann, Neville R. Kallenbach

Chemistry

Research output: Contribution to journal › Article › peer-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 homopolyribonucleotides^1,2. 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 language	English (US)
Pages (from-to)	452-454
Number of pages	3
Journal	Nature
Volume	254
Issue number	5499
DOIs	https://doi.org/10.1038/254452a0
State	Published - 1975

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title = "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.",

author = "Gabriel Kaufmann and Kallenbach, {Neville R.}",

year = "1975",

doi = "10.1038/254452a0",

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journal = "Nature",

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AU - Kaufmann, Gabriel

AU - Kallenbach, Neville R.

PY - 1975

Y1 - 1975

N2 - 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.

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

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