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Differential effects of various double-stranded RNAs on protein synthesis in rabbit reticulocyte lysates

par Content, Jean ;Lebleu, Bernard ;de Clercq, Erik
Référence Biochemistry, 17, 1, page (88-94)
Publication Publié, 1978

Article révisé par les pairs

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Résumé :

There exist remarkable differences in the ability of various double-stranded RNAs (ds RNAs) to inhibit protein synthesis in rabbit reticulocyte lysates. Natural ds RNAs (either mycophage, bacteriophage, or reovirus ds RNA) are extremely potent inhibitors of protein synthesis, effecting nearly 90% inhibition at a concentration as low as 10 ng/mL. A similar inhibitory potency is exhibited by the alternating copolymer (A-U)n·(A-U)n. However, homopolynucleotide pairs such as (A)n·(U)n and (I)n·(C)n are much less efficient inhibitors. To achieve an inhibitory effect with these homopolymer pairs, 10- to 100-fold higher concentrations were required than for the natural ds RNAs and the extent of inhibition never exceeded 50-60%. In some reticulocyte lysates (I)n·(C)n was totally inactive in inhibiting protein synthesis. Two analogues of (I)n·(C)n, (I)n·(br5C)n, and (I)n·(s2C)n were also inactive in inhibiting protein synthesis even at con-centrations up to 10 μg/mL. In some aspects, e.g., molecular size, the interferon inducing capacity of ds RNAs and their inhibitory effect on protein synthesis appear to be governed by the same structural parameters. However, the observation that the natural ds RNAs, while much more efficient as inhibitors of protein synthesis (in rabbit reticulocyte lysates), proved considerably less effective in inducing interferon (in primary rabbit kidney cell cultures) than their homopolymer counterparts [(I)n·(C)n, (I)n·(br5C)n, (I)n·(s2C)n] clearly indicates that the fine structural requirements underlying the interferon inducing and protein synthesis inhibiting properties of ds RNAs are not identical. © 1978 American Chemical Society.