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Nucleic Acids Research, 1981, Vol. 9, No. 1 189-201
© 1981

CHEMISTRY

Some substrate properties of analogues of oligothymidylates with p-s-C5' bonds

V.N. Rybakov, M.I. Rivkin and V.P. Kumarev

Institute of Cytology and Genetics, Siberian Division of the Academy of Sciences Novosibirsk 90, USSR

Received September 17, 1980. The action of T4 polynucleotide kinase, T4 DNA polymerase, E.coli DBA polymerase I, snake venom phosphodiesterase (VPDE) and S1 nuclease on analogues of oligothymidilates with. p-s-C5' bonds and the ability of these analogues to prime the replication of poly (dA) by T4 DNA polymerase were studied. These analogues were shown to be substrates for all these enzymes. Substitution of these analogues for corresponding oligothymidilates in the reaction mixtures resulted in drop in rates of enzymic reactions. This drop in reactions rates was not significant when these oligonucleotides were phosphorylated with T4 polynucleotide kinase or used as a primers, however in comparison with oligothymidilates these analogues were found to be considerably more resistant to nucleolytic hydrolysis. Some possible applications of these analogues are discussed.


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