Abstract
In a previous study (1–3), we found that terminal deoxyribonucleotidyl transferase (TdT), DNA polymerase α, DNA polymerase β, and DNA ligase II were markedly inhibited when incubated in a reconstituted poly(ADP-ribosyl)ating enzyme system. We have reported also the direct evidence for poly(ADP-ribosyl)ation of TdT (2) and DNA polymerase β (3). Based on these results, we proposed that a role of poly(ADP-ribose) synthetase in DNA repair is to cause an emergency halt of chromatin function at the damaged site to protect cells from abnormal metabolism in the chromatin (4).
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Yoshihara, K. et al. (1989). In Vitro Evidence for Poly(ADP-Ribosyl)ation of DNA Polymerase α-Primase and Phosphorylation of Poly(ADP-Ribose) Synthetase by Protein Kinase C. In: Jacobson, M.K., Jacobson, E.L. (eds) ADP-Ribose Transfer Reactions. Springer, New York, NY. https://doi.org/10.1007/978-1-4615-8507-7_7
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DOI: https://doi.org/10.1007/978-1-4615-8507-7_7
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