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2',5' A synthetase: allosteric activation by fructose 1,6-bisphosphate
R J Suhadolnik1, S W Li, R W Sobol
1Department of Biochemistry, Temple University School of Medicine, Philadelphia, Pennsylvania 19140.
Biochemical and Biophysical Research Communications
|June 29, 1990
Abstract:
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.