Abstract
2′,5′-Oligoadenylate (2-5A)-dependent RNase (L or F) is the final enzyme in the 2-5A pathway and a key component in the molecular mechanism of interferon (IFN) action. Here we demonstrate differences in the 2-5A oligomer size requirement between rabbit 2-5A-dependent RNase from reticulocytes and from cultured kidney cells. The rabbit reticulocyte enzyme was activated by tetramer 2-5A, whereas the ribonuclease from rabbit kidney cells required only trimer 2-5A. Interestingly, in contrast to the 2-5A-dependent RNase from rabbit reticulocytes, that from murine reticulocytes could be activated by trimer 2-5A. Partial proteolysis of affinity-labeled, 80-kD 2-5A-dependent RNase from rabbit reticulocytes and rabbit kidney cells resulted in the same pattern of labeled peptides. However, the affinity labeling reaction with a 32P-labeled 2-5A analog did produce some different labeled polypeptides in rabbit kidney cell extract and rabbit reticulocyte lysate. These results could indicate specialized functions for the 2-5A system in different organ systems.
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