| Literature DB >> 30713098 |
Yunsu Jang1, Heyjin Son1, Sang-Wook Lee2, Wonseok Hwang2, Seung-Ryoung Jung2, Jo Ann W Byl3, Neil Osheroff4, Sanghwa Lee5.
Abstract
Topoisomerase II cleaves DNA at preferred sequences with different efficiencies; however, the mechanism of cleavage site selection is not known. Here we used single-molecule fluorescence assays that monitor several critical steps of DNA-topoisomerase II interactions, including binding/dissociation, bending/straightening, and cleavage/religation, and reveal that the cleavage site is selected mainly during the bending step. Furthermore, despite the sensitivity of the bending rate to the DNA sequence, it is not an intrinsic property of the DNA itself. Rather, it is determined by protein-DNA interactions.Entities:
Keywords: DNA bending; DNA cleavage; DNA flexibility; G-segment selection; sequence preference; single-molecule FRET; topoisomerase II; two-metal-ion mechanism
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Year: 2019 PMID： 30713098 PMCID： PMC6474810 DOI： 10.1016/j.chembiol.2018.12.003
Source DB: PubMed Journal: Cell Chem Biol ISSN： 2451-9448 Impact factor: 8.116