Topoisomerase II is a structural component of mitotic chromosome scaffolds.

William C. Earnshaw(Johns Hopkins University), Brian Halligan(Johns Hopkins University), Carol Cooke(Johns Hopkins University), Margarete M. S. Heck(Johns Hopkins University), Leroy F. Liu(Johns Hopkins University)
The Journal of Cell Biology
May 1, 1985
Cited by 760Open Access
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Abstract

We have obtained a polyclonal antibody that recognizes a major polypeptide component of chicken mitotic chromosome scaffolds. This polypeptide migrates in SDS PAGE with Mr 170,000. Indirect immunofluorescence and subcellular fractionation experiments confirm that it is present in both mitotic chromosomes and interphase nuclei. Two lines of evidence suggest that this protein is DNA topoisomerase II, an abundant nuclear enzyme that controls DNA topological states: anti-scaffold antibody inhibits the strand-passing activity of DNA topoisomerase II; and both anti-scaffold antibody and an independent antibody raised against purified bovine topoisomerase II recognize identical partial proteolysis fragments of the 170,000-mol-wt scaffold protein in immunoblots. Our results suggest that topoisomerase II may be an enzyme that is also a structural protein of interphase nuclei and mitotic chromosomes.


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