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. 1974 Sep;71(9):3741–3745. doi: 10.1073/pnas.71.9.3741

Covalent Joining of Phenylalanine Transfer Ribonucleic Acid Half-Molecules by T4 RNA Ligase

Gabriel Kaufmann 1, Uriel Z Littauer 1
PMCID: PMC433852  PMID: 4610584

Abstract

RNA ligase from T4-phage-infected Escherichia coli cells catalyzes the covalent joining of two polynucleotides that are partially hydrogen-bonded to each other. Two polynucleotide fragments derived from yeast tRNAPhe and consisting of residues 1-36 and 38-74 are covalently joined by the enzyme. The product of the reaction lacks residue Y37 and has an anticodon loop with six nucleotide residues, whereas all tRNA species whose sequences have so far been determined have seven nucleotides in this loop.

Evidence is also presented for the formation of a polynucleotide-adenylylate intermediate in the joining reaction, in which a pyrophosphate bond links the 5′-phosphoryl terminus of the polynucleotide and the phosphoryl group of AMP.

Keywords: polyribonucleotide synthesis, anticodon loop, adenylylated polyribonucleotides

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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