Polynucleotide ligase-catalyzed joining of deoxyribo-oligonucleotides on ribopolynucleotide templates and of ribo-oligonucleotides on deoxyribopolynucleotide templates.

نویسندگان

  • K Kleppe
  • J H Van de Sande
  • H G Khorana
چکیده

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.

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عنوان ژورنال:
  • Proceedings of the National Academy of Sciences of the United States of America

دوره 67 1  شماره 

صفحات  -

تاریخ انتشار 1970