J. Biol. Chem., Vol. 260, Issue 6, 3666-3671, Mar, 1985
Cordycepin analogs of ppp5'A2'p5'A2'p5'A (2-5A) inhibit protein synthesis through activation of the 2-5A-dependent endonuclease
DA Eppstein, MA Van der Pas, BB Schryver, H Sawai, K Lesiak, J Imai and PF Torrence
Analogs of the triphosphate 2'-5'-linked adenylate trimer
(ppp5'A2'p5'A2'p5'A, called 2-5A) which contain 3'-deoxyadenosine
(cordycepin) instead of adenosine either in positions one and two, or in
all three positions, are 10-100-fold less potent than is parent 2-5A in
inhibition of protein synthesis in intact cells, when utilizing calcium
co-precipitation techniques to introduce the 5'-triphosphate
oligonucleotides into the cells. That the inhibition of protein synthesis
was a consequence of activation of the 2-5A-dependent endonuclease by the
3'-deoxyadenosine analogs of 2-5A was demonstrated in obtaining the
ribosomal RNA cleavage pattern that is characteristic of endonuclease
activation by parent 2-5A. Additional results (i.e. lack of activity by the
dimer species ppp5'(3'dA)2'p5'-(3'dA) or the monomer 3'dA) as well as
kinetic analysis both in intact cells and in cell-free extracts provided
further evidence that the inhibition of protein synthesis observed with
these 3'-deoxyadenosine 2-5A analogs was not due to their degradation to
the antimetabolite monomer unit 3'- deoxyadenosine.
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