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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. 1 — a (i) Domain model of human (hs) TopBP1, its conservation with BRCT1/2 and 3/4 domains (grey boxes) of budding yeast Dpb11 (scDpb11). Arrows point to binding domains for interacting proteins. (ii) Overview of TopBP1 wild type (WT) and BRCT deletion (Δ) and point mutants. GINS binding capabilities are labelled in red and green. Numbers, amino acid position; capital letters indicate amino acid substitutions. Amino acid substitutions of point mutants in BRCT4 (B4mut) and 5 (B5mut) are coloured orange. b Elution profiles of size exclusion chromatography (Superdex200) of individual recombinant TopBP1-BRCT0-5 protein (grey) and GINS tetramers (green), or of both upon incubation (blue). c Recombinant GINS immobilised on Flag-beads and control beads (Flag peptide-coupled beads) were used to pull down recombinant TopBP1-0-5-WT or TopBP1-ΔBRCT4/5 (compare a(ii)). SDS gels were silver stained. kDa specifies molecular weight marker bands. The experiment was done more than three times with similar results. Source data are provided as a Source data file.