Phosphorylation of DNA topoisomerase II in vivo and in total homogenates of Drosophila Kc cells. The role of casein kinase II.

@article{Ackerman1988PhosphorylationOD,
  title={Phosphorylation of DNA topoisomerase II in vivo and in total homogenates of Drosophila Kc cells. The role of casein kinase II.},
  author={Phillip Ackerman and Claiborne V. C. Glover and Neil Osheroff},
  journal={The Journal of biological chemistry},
  year={1988},
  volume={263 25},
  pages={12653-60}
}
The phosphorylation of DNA topoisomerase II in Drosophila Kc tissue culture cells was characterized by in vivo labeling studies and in vitro studies that examined the modification of exogenous enzyme in total homogenates of these embryonic cells. Several lines of evidence identified casein kinase II as the kinase primarily responsible for phosphorylating DNA topoisomerase II. First, the only amino acyl residue modified in the enzyme was serine. Second, partial proteolytic maps of topoisomerase… CONTINUE READING

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