Extended Data Fig. 1. Biochemical and cellular characterizations of various Vif–CBFβ–A3F_CTDm assemblies and the A3F_CTDm-CBFβ interaction.

a, The Vif–CBFβ–A3F_CTDm fusion complex with or without the Vif α-domain and corresponding interacting CBFβ C-terminus stays as tetramer in low salt solution. The unfused Vif–CBFβ–A3F_CTDm without these regions switches from monomer to tetramer at high protein concentration (146 μΜ loading concentration). b, No obvious shift for the elution peak was observed upon incubation of CBFβ and A3F_CTDm compared to the CBFβ alone or A3F_CTDm alone. The SDS-PAGE analysis of the peak fractions of CBFβ alone, A3F_CTDm alone and CBFβ/A3F_CTDm mixture is indicated. c, Co-immunoprecipitation (Co-IP) analysis of the interaction between A3F and CBFβ in the presence or absence of Vif in cells. Flag-A3F and CBFβ-myc were co-transfected with or without Vif-HA and co-immunoprecipitated using anti-Flag antibody. In the absence of Vif, no binary A3F and CBFβ binding was observed. A representative blot from two independent experiments was shown.