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. 2024 Feb 27;15:1797. doi: 10.1038/s41467-024-45946-0

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — a Structural model of the GINS-TopBP1-BRCT4/5 complex. Crystal structures of the GINS subunits (PDB:2E9X) (shades of green, yellow), and the central BRCT4/5 domain of TopBP1 (PDB:3UEN) (grey) were docked into the cryo-EM volume shown as transparent volume. b Zoom-in of the BRCT4-Psf1 interface. The residues in stick representation appear crucial for the interface. Mutations to break the interaction are coloured pink (Psf1-I97R) and purple (TopBP1-B4mut; compare Fig. 1a(ii)). c Pulldown of the indicated recombinant TopBP1-BRCT0-5-strep versions (see Fig. 1a(ii)) by Flag-beads-immobilised recombinant GINS or Flag peptide-coupled control beads. Analysis was done by immunoblotting. The experiment was done more than three times with similar results. d Pulldown of the indicated recombinant TopBP1-BRCT0-5-WT-strep using immobilised GINS-WT or GINS carrying a Ile97 to arginine mutation in Psf1.TopBP1-Gcc/B4mut-strep (Figs. 1a(ii) and 3a) was used as a non-GINS binding control. The experiment was done twice with similar results. Source data are provided as a Source data file.