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Interferon action: two (2'-5')(A)n synthetases specified by distinct mRNAs in Ehrlich ascites tumor cells treated

G St Laurent, O Yoshie, G Floyd-Smith

    Cell
    |May 1, 1983
    PubMed

    Insights

    Interferons induce two (2'-5')(A)n synthetase mRNAs in tumor cells, producing enzymes that activate RNAase L. These enzymes, differing in size and cellular location, are key mediators of interferon's antiviral action.

    Area of Science:

    • Molecular Biology
    • Virology
    • Biochemistry

    Background:

    • Interferons mediate antiviral responses through complex signaling pathways.
    • 2-5 oligoadenylate synthetase ((2 -5 )(A)n synthetase) and RNAase L are key enzymes in interferon action.
    • 2-5 oligoadenylate ((2 -5 )(A)n) activates RNAase L, a latent endoribonuclease.

    Purpose of the Study:

    • To investigate the interferon-induced (2 -5 )(A)n synthetases in Ehrlich ascites tumor (EAT) cells.
    • To characterize the sizes and cellular localization of these synthetases.
    • To explore the interaction between (2 -5 )(A)n and RNAase L in different cellular fractions.

    Main Methods:

    • Induction of mRNAs and protein synthesis in EAT cells by interferons.
    • Translation of EAT cell mRNAs in Xenopus oocytes to determine synthetase sizes.
    • Cellular fractionation to isolate cytoplasmic and nuclear extracts.
    • Crosslinking studies to investigate protein-RNA interactions with (2 -5 )(A)n derivatives.

    Main Results:

    • Interferons induced two mRNAs (1.5 kb and 3.8 kb) in EAT cells, translating to synthetases of 20-30 kDa and 85-100 kDa.
    • The larger synthetase was predominantly in the cytoplasmic fraction, while the smaller was in the nuclear fraction.
    • RNAase L was crosslinked to a (2 -5 )(A)n derivative in cytoplasmic extracts.
    • Multiple interferon-induced proteins were crosslinked to the (2 -5 )(A)n derivative in nuclear extracts.

    Conclusions:

    • Interferons induce distinct (2 -5 )(A)n synthetases of different sizes and subcellular localizations in EAT cells.
    • These synthetases play a role in activating RNAase L, a crucial component of the interferon antiviral response.
    • The findings highlight the complexity of interferon-mediated signaling and RNA processing.

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