An interferon-induced phosphodiesterase degrading (2'-5') oligoisoadenylate and the C-C-A terminus of tRNA.
A phosphodiesterase characterized by a generally higher activity on 2'-5' than on 3'-5' phosphodiester bonds was isolated from mouse L cells treated with interferon. A similar enzyme was purified from mouse reticulocytes. The phosphodiesterase 2'-PDi splits the 2'-phosphate bond of pppA2'p5'A2'p5'A, the oligonucleotide activator of ribonuclease F. The level of phosphodiesterase 2'-PDi is increased by interferon treatment of L cells. The phosphodiesterase was also shown to degrade the C-C-A terminus of tRNA and to reduce the amino acid acceptance of tRNA in cell-free extracts, thereby causing a tRNA-reversible inhibition of mRNA translation.
D000604:Amino Acyl-tRNA Synthetases / Q000378:metabolism; D000818:Animals; D007372:Interferons / Q000494:pharmacology*; D007739:L Cells / Q000201:enzymology; D051379:Mice; D009843:Oligoribonucleotides; D010727:Phosphoric Diester Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D012343:RNA, Transfer; D011817:Rabbits; D012156:Reticulocytes / Q000201:enzymology; D013379:Substrate Specificity
D009843:Oligoribonucleotides; D007372:Interferons; D012343:RNA, Transfer; D010727:Phosphoric Diester Hydrolases; D000604:Amino Acyl-tRNA Synthetases