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- W3005514963 abstract "Type IA DNA topoisomerases (Topo IA) are ubiquitous enzymes conserved from bacteria to humans. Topo IA enzymes share a common toroidal architecture that binds and cleaves a single-stranded DNA and passes a second segment of single-stranded DNA through a transient protein-mediated DNA gate. E. coli possess two Topo IA enzymes; topoisomerase I (top1) and III (top3). Despite their shared catalytic mechanism and structural similarity, the two enzymes play distinct roles in vivo: top1 is involved in reducing hyper-negative supercoils whereas top3 resolves replication intermediates and other linked DNA structures. The functional differences between top1 and top3 can be generally attributed to differences in their protein sequence and domain structure, but the physical and chemical differences between the two enzymes that modulate their activities remain unclear. In this study, we investigated the relaxation and decatenation activities of top1 and top3 using magnetic tweezers while varying the Mg2+ concentration, force, and torque on the DNA. Our results show that the rates of supercoil relaxation of top1 and top3 are comparable in the low DNA torque regime. However, top1 is highly efficient at relaxing hyper-negatively supercoiled DNA whereas top3 maintains higher rates of relaxation and decatenation than top1 as the torque or tension on the DNA are increased. Based on steered molecular dynamic simulations, we found that these catalytic differences between top1 and top3 likely originate from differences in the structural rigidity of their gate domains. Our experimental and computational study suggests how these two closely related enzymes evolved to achieve their distinct physiological functions." @default.
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- W3005514963 date "2020-02-01" @default.
- W3005514963 modified "2023-09-26" @default.
- W3005514963 title "Domain Rigidity Modulates the Catalytic Activity of E. coli Type IA DNA Topoisomerases" @default.
- W3005514963 doi "https://doi.org/10.1016/j.bpj.2019.11.570" @default.
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