Chromatinization modulates topoisomerase II processivity

Jaeyoon Lee, Meiling Wu, James T. Inman, Gundeep Singh, Seong ha Park, Joyce H. Lee, Robert M. Fulbright, Yifeng Hong, Joshua Jeong, James M. Berger and Michelle D. Wang ()
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Jaeyoon Lee: Cornell University
Meiling Wu: Cornell University
James T. Inman: Cornell University
Gundeep Singh: Cornell University
Seong ha Park: Cornell University
Joyce H. Lee: Johns Hopkins University School of Medicine
Robert M. Fulbright: Cornell University
Yifeng Hong: Cornell University
Joshua Jeong: Johns Hopkins University School of Medicine
James M. Berger: Johns Hopkins University School of Medicine
Michelle D. Wang: Cornell University

Nature Communications, 2023, vol. 14, issue 1, 1-17

Abstract: Abstract Type IIA topoisomerases are essential DNA processing enzymes that must robustly and reliably relax DNA torsional stress. While cellular processes constantly create varying torsional stress, how this variation impacts type IIA topoisomerase function remains obscure. Using multiple single-molecule approaches, we examined the torsional dependence of eukaryotic topoisomerase II (topo II) activity on naked DNA and chromatin. We observed that topo II is ~50-fold more processive on buckled DNA than previously estimated. We further discovered that topo II relaxes supercoiled DNA prior to plectoneme formation, but with processivity reduced by ~100-fold. This relaxation decreases with diminishing torsion, consistent with topo II capturing transient DNA loops. Topo II retains high processivity on buckled chromatin (~10,000 turns) and becomes highly processive even on chromatin under low torsional stress (~1000 turns), consistent with chromatin’s predisposition to readily form DNA crossings. This work establishes that chromatin is a major stimulant of topo II function.

Date: 2023
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DOI: 10.1038/s41467-023-42600-z

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