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. 1981 May 29;212(4498):1030-2.
doi: 10.1126/science.6165080.

Interferon action: RNA cleavage pattern of a (2'-5')oligoadenylate--dependent endonuclease

G Floyd-Smith, E Slattery, P Lengyel

Interferon action: RNA cleavage pattern of a (2'-5')oligoadenylate--dependent endonuclease

G Floyd-Smith et al. Science. .

Abstract

One of the mediators of interferon action is a latent endoribonuclease (ribonuclease L) that is activated by (2'-5')oligoadenylates. Among the homopolymers of the four common ribonucleotides, activated ribonuclease L degrades at an appreciable rate only polyuridylic acid. In two natural RNA's tested the most frequent ribonuclease L cleavages occur after UA, UG, and UU (A, adenine; U, uracil; and G, guanine) and much less frequent cleavages after CA and AC (C, cytosine).

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