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J. Biol. Chem., Vol. 262, Issue 8, 3852-3857, 03, 1987
J Chebath, P Benech, A Hovanessian, J Galabru and M Revel
Antibodies against synthetic peptides derived from the cDNA sequence of
interferon-induced 2',5'-oligo(A) synthetase, and which immunoprecipitate
the native enzyme activity, were found to detect multiple enzyme forms in
denaturing electrophoretic immunoblots. In some human cell lines, four
different interferon-induced proteins of 40, 46, 67, and 100 kDa were found
to react with the same peptide antibodies. Each isolated form was shown to
have 2',5'-oligo(A) synthetase activity, but the dependence on
double-stranded RNA was markedly different for activation of the individual
enzymes. The four enzyme forms also differ in their intracellular
localization, on microsomes (100 kDa), in nuclei (67, 46, 40 kDa), and on
membrane structures (67 kDa). Plasma membranes from interferon-treated
Daudi lymphoblastoid cells are highly enriched in the 67-kDa 2',5'-oligo(A)
synthetase form. The 2',5'-oligo(A) synthetase activity induced by
interferons in human cells appears, therefore, as a complex multienzyme
system.
Four different forms of interferon-induced 2',5'-oligo(A) synthetase identified by immunoblotting in human cells
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