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

Greta Bianchi (1) , Marco Mangiagalli (1) , Diletta Ami (1) , Junaid Ahmed (2) , Silvia Lombardi (1) , Sonia Longhi (3) , Antonino Natalello (1) , Peter Tompa (2) , Stefania Brocca (1)

1 UNIMIB - Università degli Studi di Milano-Bicocca = University of Milano-Bicocca
2 VUB - Vrije Universiteit Brussel [Bruxelles]
3 AFMB - Architecture et fonction des macromolécules biologiques

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]

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⟩