Fig. 5: Characterization of the Brr1 structure.
a Secondary structural elements of human Gemin2 and S. cerevisiae Brr1. Known domain compositions are indicated. b Superimposition of the AlphaFold and RosettaFold models of Brr1(80-341). c The summary of the truncated constructs of Brr1CD and expression test results. See details in Supplementary Fig. 7. d The superimposition of the AlphaFold structure model of Brr1(80-341) (colored in rainbow: the N-terminus in blue, the C-terminus in red) with the structure of human Gemin2-CD (in light gray, PDB: 5XJL). The superimposition reveals that the long loop between α7 and α8 in Brr1 (in orange), which contains αE, occupies the position where SMNGe2BD (in dark gray) binds to Gemin2. Moreover, the EHD of Brr1 is far away from SmD1/D2. e The binding assay was conducted to test the interaction of Brr1Δ(122-197) with each of the three Sm subcomplexes, individually and together. The interaction was assessed using a pull-down assay with Ni-beads. One representative of two independent experiments is shown. M markers.
