Suhadolnik R J, Li S W, Sobol R W, Varnum J M
Department of Biochemistry, Temple University School of Medicine, Philadelphia, Pennsylvania 19140.
Biochem Biophys Res Commun. 1990 Jun 29;169(3):1198-203. doi: 10.1016/0006-291x(90)92023-s.
Fructose 1,6-bisphosphate (fru-1,6-P2), but not other glycolytic intermediates, activates highly purified 2',5' A synthetases from rabbit reticulocyte lysates and from 2',5'-ADP-agarose purified extracts of interferon-treated HeLa cells without the addition of dsRNA. The 2',5' A was structurally and biologically identical to authentic 2',5' A. Micrococcal nuclease inhibited the activation of 2',5' A synthetase by poly(I)-poly(C), but did not affect activation by fru-1,6-P2. Addition of fru-1,6-P2 aldolase prevented the activation of 2',5' A synthetase by fru-1,6-P2.
