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.
Domains
Life Sciences [q-bio]Origin | Files produced by the author(s) |
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