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Nucleic Acids Research, 1982, Vol. 10, No. 6 2163-2174
© 1982

MOLECULAR BIOLOGY

Structural requirements of (2'–5') oligoadenylate for protein synthesis inhibition in human fibroblasts

J.-L. Drocourt, C.W. Dieffenbach, P.O.P. Ts'o, J. Justesen and M.N. Thang

Division of Biophysics, The Johns Hopkins University, School of Hygiene and Public Health 615 N.Wolfe Street, Baltimore, MD 21205, USA Institut de Biologie Physico-Chimique, Fondation Edmond de Rothschild 13, Rue Pierre et Marie Curie, 75005 Paris, France

Received December 29, 1981. Revised February 23, 1982. Accepted February 26, 1982.

The structural requirements of (2'–5')-oligoadenylic add (pppA(2'p5'A)x, x>1 or ('–5')An) for inhibition of protein synthesis in cells were examined with a modified calcium-coprecipitation technique, using a series of trinucleotide analogs (pppA2'p5'A2'p5'N, N=rC, rG, rU, T, dC, dG, dA). In this system, both the degree and the duration of the inhibition of protein synthesis were dependent on the added concentration of ('–5')A3. Of all the heterotrimers, only the deoxy A derivative was active as an inhibitor of protein synthesis, while the other members of the analog series were found to have no inhibitory effects. In competition experiments between ('–5')A3 and the non-active analogs, three heterotrimers were shown to reduce the activity of ('–5')A3 in protein inhibition. In contrast, the dephosphorylated ('–5')A3 had no inhibitory effect and was not effective in blocking ('–5')A3. These results indicate that the 5'-terminal triphosphate is important for binding of ('–5')A3 to the site of ('–5')An action and the adenine base at the 2'-terminus is important for activating the machinery responsible for protein synthesis inhibition in the cells, most likely the ('–5')An-activated nuclease.


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