Fig. 3: Characterization of the interaction between MCM8IP and MCM8-9.

a Venn diagram of the number of proteins identified by mass spectrometry that were enriched in BirA*-MCM8IP and MCM8IP-BirA* streptavidin pulldowns from HEK293T T-REx cells or MCM8IP-HA immunoprecipitates from HEK293T cells relative to their respective controls. Proteins with multiple enriched isoforms were considered a single hit in this diagram. A list of proteins commonly identified by all three experiments is presented. See also Supplementary Data 2. b Detection by western blot of MCM8 and MCM9 co-immunoprecipitated by HA-GFP, HA-MCM8IP WT, or RBM from HEK293T cells. c Schematic representation of MCM8IP truncation mutants used to identify the region of interaction with MCM8-9. d Detection by western blot of MCM8, MCM9, and RPA1 co-immunoprecipitated from HEK293T cells by HA-GFP, HA-MCM8IP WT, and mutants presented in (c). e Alignment from various species of the minimal region of human MCM8IP required for MCM8-9 interaction. MCM8IP MBM #1 mutant carries alanine substitutions of the indicated residues. MCM8IP MBM #2 mutant carries a deletion of the indicated 18 amino acid residues. Sequence alignments were conducted using Clustal Omega and processed using ESPript. f Detection by western blot of MCM8 and MCM9 co-immunoprecipitated by HA-GFP, HA-MCM8IP WT, MBM #1 or MBM #2 from HEK293T cells.