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

Jongstra-Bilen, Jenny; Ittel, Marie‐Elisabeth; Niedergang, Claude; Vosberg, Hans-Peter; Mandel, Paul

doi:10.1111/j.1432-1033.1983.tb07754.x

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

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Vosberg, Hans-Peter
Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society;

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https://febs.onlinelibrary.wiley.com/doi/epdf/10.1111/j.1432-1033.1983.tb07754.x
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https://doi.org/10.1111/j.1432-1033.1983.tb07754.x
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引用

Jongstra-Bilen, J., Ittel, M., Niedergang, C., Vosberg, H.-P., & Mandel, P. (1983). DNA topoisomerase I from calf thymus is inhibited in vitro by poly(ADP-ribosylation). European Journal of Biochemistry, 136(2), 391-396. doi:10.1111/j.1432-1033.1983.tb07754.x.

引用: https://hdl.handle.net/21.11116/0000-0003-5ACF-0

要旨

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.