DNA topoisomerase I from calf thymus is inhibited in vitro by poly(ADP‐ribosylation)

作者：Jenny Jongstra‐Bilen, M.E. Ittel, Claude Niedergang, Hans-Peter Vosberg, Paul Mandel · 发表于：European Journal of Biochemistry · 年份：1983 · DOI：10.1111/j.1432-1033.1983.tb07754.x · 被引用次数：87 · 研究领域：Cancer therapeutics and mechanisms、Cancer Treatment and Pharmacology、Synthesis and bioactivity of alkaloids

A slight DNA topoisomerase I activity was detected in highly purified poly(ADP-Rib)polymerase prepared from calf thymus. This copurified activity was found to be suppressed under conditions where the poly(ADP-ribosylation) reaction occurs in the presence of NAD. Purified topoisomerase I from calf thymus was shown to be ADP-ribosylated by poly(ADP-Rib) polymerase purified from the same tissue. Poly(ADP-ribosylation) of topoisomerase I produces an inhibition of the enzymatic activity in parallel to the extent of ADP-ribosylation. The fact that a slight poly(ADP-Rib) polymerase activity was also found to copurify with a topoisomerase I preparation and that topoisomerase I activity can be modified by ADP-ribosylation, may suggest a spatial and functional correlation of these two enzymes in chromatin.