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Fig. 3 | Physical and functional interaction of EXO1 with MutSγ depends on residues 353–390 in EXO1. a Protein interaction assays of MutSγ and EXO1 (D173A) with or without MutLγ. MutSγ <t>(MSH4-Strep-MSH5-his)</t> (bait) wasimmobilized using an anti-His antibody, and <t>EXO1</t> <t>(D173A)-FLAG</t> and MutLγ (FLAG-MLH1-MBP-MLH3) (preys) were subsequently added. Top, a schematic. Bottom, a representative of two independent experiments. b Protein interaction assay of MutSγ and EXO1 (D173A). MutSγ (MSH4-Strep-MSH5-His) (bait) was immobilized using Strep resin and EXO1 (D173A)-FLAG (prey) was subsequently added. Top, a schematic. Bottom, a representative of three Western blot. c Protein interaction assay of MutSγ and EXO1 (D173A). EXO1 (D173A)-FLAG (bait) was immobilized using anti-FLAG resin and MutSγ (MSH4-Strep-MSH5-His) (prey) was subsequently added. Top, a sche- matic. Bottom, a representative of two independent experiments. d Molecular weight distributions of EXO1 (D173A)-FLAG and/or MutSγ (MSH4-Strep-MSH5-His) measured by mass photometry. Error, SD. e A schematic overview of EXO1 (D173A) protein variants. The N-terminal catalytic domain is shown in purple, and the C-terminal tail is shown in magenta. Top, EXO1 protein with important functional
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Fig. 3 | Physical and functional interaction of EXO1 <t>with</t> <t>MutSγ</t> depends on residues 353–390 in EXO1. a Protein interaction assays of MutSγ and EXO1 (D173A) with or without MutLγ. MutSγ <t>(MSH4-Strep-MSH5-his)</t> (bait) wasimmobilized using an anti-His antibody, and EXO1 (D173A)-FLAG and MutLγ (FLAG-MLH1-MBP-MLH3) (preys) were subsequently added. Top, a schematic. Bottom, a representative of two independent experiments. b Protein interaction assay of MutSγ and EXO1 (D173A). MutSγ (MSH4-Strep-MSH5-His) (bait) was immobilized using Strep resin and EXO1 (D173A)-FLAG (prey) was subsequently added. Top, a schematic. Bottom, a representative of three Western blot. c Protein interaction assay of MutSγ and EXO1 (D173A). EXO1 (D173A)-FLAG (bait) was immobilized using anti-FLAG resin and MutSγ (MSH4-Strep-MSH5-His) (prey) was subsequently added. Top, a sche- matic. Bottom, a representative of two independent experiments. d Molecular weight distributions of EXO1 (D173A)-FLAG and/or MutSγ (MSH4-Strep-MSH5-His) measured by mass photometry. Error, SD. e A schematic overview of EXO1 (D173A) protein variants. The N-terminal catalytic domain is shown in purple, and the C-terminal tail is shown in magenta. Top, EXO1 protein with important functional
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Fig. 3 | Physical and functional interaction of EXO1 with MutSγ depends on residues 353–390 in EXO1. a Protein interaction assays of MutSγ and EXO1 (D173A) with or without MutLγ. MutSγ (MSH4-Strep-MSH5-his) (bait) wasimmobilized using an anti-His antibody, and EXO1 (D173A)-FLAG and MutLγ (FLAG-MLH1-MBP-MLH3) (preys) were subsequently added. Top, a schematic. Bottom, a representative of two independent experiments. b Protein interaction assay of MutSγ and EXO1 (D173A). MutSγ (MSH4-Strep-MSH5-His) (bait) was immobilized using Strep resin and EXO1 (D173A)-FLAG (prey) was subsequently added. Top, a schematic. Bottom, a representative of three Western blot. c Protein interaction assay of MutSγ and EXO1 (D173A). EXO1 (D173A)-FLAG (bait) was immobilized using anti-FLAG resin and MutSγ (MSH4-Strep-MSH5-His) (prey) was subsequently added. Top, a sche- matic. Bottom, a representative of two independent experiments. d Molecular weight distributions of EXO1 (D173A)-FLAG and/or MutSγ (MSH4-Strep-MSH5-His) measured by mass photometry. Error, SD. e A schematic overview of EXO1 (D173A) protein variants. The N-terminal catalytic domain is shown in purple, and the C-terminal tail is shown in magenta. Top, EXO1 protein with important functional

Journal: Nature communications

Article Title: EXO1 promotes the meiotic MLH1-MLH3 endonuclease through conserved interactions with MLH1, MSH4 and DNA.

doi: 10.1038/s41467-025-59470-2

Figure Lengend Snippet: Fig. 3 | Physical and functional interaction of EXO1 with MutSγ depends on residues 353–390 in EXO1. a Protein interaction assays of MutSγ and EXO1 (D173A) with or without MutLγ. MutSγ (MSH4-Strep-MSH5-his) (bait) wasimmobilized using an anti-His antibody, and EXO1 (D173A)-FLAG and MutLγ (FLAG-MLH1-MBP-MLH3) (preys) were subsequently added. Top, a schematic. Bottom, a representative of two independent experiments. b Protein interaction assay of MutSγ and EXO1 (D173A). MutSγ (MSH4-Strep-MSH5-His) (bait) was immobilized using Strep resin and EXO1 (D173A)-FLAG (prey) was subsequently added. Top, a schematic. Bottom, a representative of three Western blot. c Protein interaction assay of MutSγ and EXO1 (D173A). EXO1 (D173A)-FLAG (bait) was immobilized using anti-FLAG resin and MutSγ (MSH4-Strep-MSH5-His) (prey) was subsequently added. Top, a sche- matic. Bottom, a representative of two independent experiments. d Molecular weight distributions of EXO1 (D173A)-FLAG and/or MutSγ (MSH4-Strep-MSH5-His) measured by mass photometry. Error, SD. e A schematic overview of EXO1 (D173A) protein variants. The N-terminal catalytic domain is shown in purple, and the C-terminal tail is shown in magenta. Top, EXO1 protein with important functional

Article Snippet: The eluate was separated on a 7.5% SDS-PAGE gel, and the proteins were detected by Western blotting with anti-FLAG rabbit (Sigma, F7425, 1:1000) to detect both EXO1 and MutLγ, with anti-STREP mouse antibody (BioRad, MCA2489, clone Strep-tag II, dilution 1:1000) to detect MSH4 in MutSγ andwith anti-Hismouse antibody (MBL, D291-3, 1:5000) to detectMSH5 of MutSγ.

Techniques: Functional Assay, Protein Interaction Assay, Western Blot, Molecular Weight

Fig. 3 | Physical and functional interaction of EXO1 with MutSγ depends on residues 353–390 in EXO1. a Protein interaction assays of MutSγ and EXO1 (D173A) with or without MutLγ. MutSγ (MSH4-Strep-MSH5-his) (bait) wasimmobilized using an anti-His antibody, and EXO1 (D173A)-FLAG and MutLγ (FLAG-MLH1-MBP-MLH3) (preys) were subsequently added. Top, a schematic. Bottom, a representative of two independent experiments. b Protein interaction assay of MutSγ and EXO1 (D173A). MutSγ (MSH4-Strep-MSH5-His) (bait) was immobilized using Strep resin and EXO1 (D173A)-FLAG (prey) was subsequently added. Top, a schematic. Bottom, a representative of three Western blot. c Protein interaction assay of MutSγ and EXO1 (D173A). EXO1 (D173A)-FLAG (bait) was immobilized using anti-FLAG resin and MutSγ (MSH4-Strep-MSH5-His) (prey) was subsequently added. Top, a sche- matic. Bottom, a representative of two independent experiments. d Molecular weight distributions of EXO1 (D173A)-FLAG and/or MutSγ (MSH4-Strep-MSH5-His) measured by mass photometry. Error, SD. e A schematic overview of EXO1 (D173A) protein variants. The N-terminal catalytic domain is shown in purple, and the C-terminal tail is shown in magenta. Top, EXO1 protein with important functional

Journal: Nature communications

Article Title: EXO1 promotes the meiotic MLH1-MLH3 endonuclease through conserved interactions with MLH1, MSH4 and DNA.

doi: 10.1038/s41467-025-59470-2

Figure Lengend Snippet: Fig. 3 | Physical and functional interaction of EXO1 with MutSγ depends on residues 353–390 in EXO1. a Protein interaction assays of MutSγ and EXO1 (D173A) with or without MutLγ. MutSγ (MSH4-Strep-MSH5-his) (bait) wasimmobilized using an anti-His antibody, and EXO1 (D173A)-FLAG and MutLγ (FLAG-MLH1-MBP-MLH3) (preys) were subsequently added. Top, a schematic. Bottom, a representative of two independent experiments. b Protein interaction assay of MutSγ and EXO1 (D173A). MutSγ (MSH4-Strep-MSH5-His) (bait) was immobilized using Strep resin and EXO1 (D173A)-FLAG (prey) was subsequently added. Top, a schematic. Bottom, a representative of three Western blot. c Protein interaction assay of MutSγ and EXO1 (D173A). EXO1 (D173A)-FLAG (bait) was immobilized using anti-FLAG resin and MutSγ (MSH4-Strep-MSH5-His) (prey) was subsequently added. Top, a sche- matic. Bottom, a representative of two independent experiments. d Molecular weight distributions of EXO1 (D173A)-FLAG and/or MutSγ (MSH4-Strep-MSH5-His) measured by mass photometry. Error, SD. e A schematic overview of EXO1 (D173A) protein variants. The N-terminal catalytic domain is shown in purple, and the C-terminal tail is shown in magenta. Top, EXO1 protein with important functional

Article Snippet: To investigate the interaction between MutSγ and EXO1 variants reciprocally, 1μg anti-STREP antibody (BioRad,MCA2489, clone Strep-tag II) was captured on 10μl protein G magnetic beads (STREP-tag is on the C-terminus ofMSH4).

Techniques: Functional Assay, Protein Interaction Assay, Western Blot, Molecular Weight