Polynucleotide Ligase-Catalyzed Joining of Deoxyribo-Oligonucleotides on Ribopolynucleotide Templates and of Ribo-Oligonucleotides on Deoxyribopolynucleotide Templates
Abstract
T4 polynucleotide ligase efficiently catalyzes the head-to-tail joining of the ribo-oligoadenylates, r-(pA)8 and r-(pA)10, in the presence of high molecular weight deoxypolythymidylate. The enzyme also catalyzes the joining of deoxy-oligothymidylates, e.g., d-(pT)10, in the presence of ribopolyadenylate. The enzyme failed to bring about the joining of r-(pA)10 when poly r-U was used as the template, although a slow formation of the expected activated intermediate from r-(pA)10 was detected.
- Publication:
-
Proceedings of the National Academy of Science
- Pub Date:
- September 1970
- DOI:
- 10.1073/pnas.67.1.68
- Bibcode:
- 1970PNAS...67...68K