Abstract
Ribonuclease activity in HeLa cell nuclei is markedly inhibited by ADP-ribosylation following incubation of intact isolated nuclei with [14C]NAD. Time course experiments demonstrate that [24C] incorporation into proteins is accompanied by a 50% inhibition of ribonuclease activity on single-strand and double-strand polynucleotides. Inhibition does not occur when 3-aminobenzamide, a potent (ADP-ribose)polymerase inhibitor, is present.
Two enzymatic activities that degrade double-strand polynucleotides have been purified and partially characterized. A relevant level of radioactivity resulting from [14C]NAD incubation of nuclei was associated to the purified enzyme. The RNase Fl component, which shows maximal activity on polyU-polyA is demonstrated to be the major ADP-ribose acceptor protein.
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Quesada, P., Merola, M., Farina, B. et al. In vitro inhibition of HeLa cell nuclear ribonucleases by ADP-ribosylation. Mol Cell Biochem 94, 53–60 (1990). https://doi.org/10.1007/BF00223562
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DOI: https://doi.org/10.1007/BF00223562