Condensation of the N-terminal domain of human topoisomerase 1 is driven by electrostatic interactions and tuned by its charge distribution - Archive ouverte HAL Access content directly
Journal Articles International Journal of Biological Macromolecules Year : 2023

Condensation of the N-terminal domain of human topoisomerase 1 is driven by electrostatic interactions and tuned by its charge distribution

Abstract

Highlights • Human topoisomerase 1 (hTOP1) can form condensates in the nucleolus and nucleoplasm; • Human topoisomerase I contains a condensation-prone, N-terminal domain (hNTD); • hNTD is highly charged and its in-vitro condensation is driven by electrostatic forces; • There is a critical charge clustering threshold affecting LLPS efficiency; • This research extends the applicability of "stickers-and-spacers" theory to supercharged IDPs.
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Monday, April 29, 2024
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Monday, April 29, 2024
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Dates and versions

hal-04277952 , version 1 (09-11-2023)

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Greta Bianchi, Marco Mangiagalli, Diletta Ami, Junaid Ahmed, Silvia Lombardi, et al.. Condensation of the N-terminal domain of human topoisomerase 1 is driven by electrostatic interactions and tuned by its charge distribution. International Journal of Biological Macromolecules, 2023, 254, pp.127754. ⟨10.1016/j.ijbiomac.2023.127754⟩. ⟨hal-04277952⟩
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