2',5' A synthetase: allosteric activation by fructose 1,6-bisphosphate.
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.
Suhadolnik
R J
RJ
Department of Biochemistry, Temple University School of Medicine, Philadelphia, Pennsylvania 19140.
Li
S W
SW
Sobol
R W
RW
Varnum
J M
JM
D015088:2',5'-Oligoadenylate Synthetase / Q000378:metabolism*; D000494:Allosteric Regulation; D000818:Animals; D004722:Endoribonucleases / Q000378:metabolism; D004789:Enzyme Activation; D005635:Fructosediphosphates / Q000494:pharmacology*; D006019:Glycolysis; D006598:Hexosediphosphates / Q000494:pharmacology*; D066298:In Vitro Techniques; D011817:Rabbits; D012156:Reticulocytes / Q000201:enzymology
D005635:Fructosediphosphates; D006598:Hexosediphosphates; D015088:2',5'-Oligoadenylate Synthetase; D004722:Endoribonucleases; C031956:2-5A-dependent ribonuclease; C029063:fructose-1,6-diphosphate