Condensation of the N-terminal domain of human topoisomerase 1 is driven by electrostatic interactions and tuned by its charge distribution
Résumé
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.
Domaines
Sciences du Vivant [q-bio]Origine | Fichiers produits par l'(les) auteur(s) |
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