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Selection of DNA Cleavage Sites by Topoisomerase II Results from Enzyme-Induced Flexibility of DNA.


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.

SUBMITTER: Jang Y 

PROVIDER: S-EPMC6474810 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature

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Selection of DNA Cleavage Sites by Topoisomerase II Results from Enzyme-Induced Flexibility of DNA.

Jang Yunsu Y   Son Heyjin H   Lee Sang-Wook SW   Hwang Wonseok W   Jung Seung-Ryoung SR   Byl Jo Ann W JAW   Osheroff Neil N   Lee Sanghwa S  

Cell chemical biology 20190131 4


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 sequen  ...[more]

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