Fig. 6
From: Structural basis of meiotic telomere attachment to the nuclear envelope by MAJIN-TERB2-TERB1
Structure of the 2:1:1 TRF1–TERB1-TERB2 complex. a Size-exclusion chromatography elution profiles of TRF1TRFH (62–268), TRF1TRFH-TERB1TRFB (62–268, 561–658) and TRF1TRFH-TERB1TRFB-TERB2N (62–268, 561–658, 1-119). A longer TERB2N construct of 1-119 was used for size exclusion chromatography and SDS–PAGE to provide molecular weight discrimination from TERB1TRFB; all other experiments use a shorter 1–107 construct. Source data are provided as a Source Data file. b SEC-MALS analysis. TRF1TRFH is a dimer (49 kDa; theoretical dimer – 48 kDa), TRF1TRFH-TERB1TRFB is 2:1 (58 kDa; theoretical 2:1–59 kDa) and TRF1TRFH-TERB1TRFB-TERB2N is 2:1:1 (84 kDa; theoretical 2:1:1–73 kDa). c, d Multi-phase SAXS ab initio modelling of TRF1TRFH-TERB1TRFB-TERB2N using MONSA in which experimental data of the complex and its constituents were used to fit their ab initio structures and relative orientations within the full complex. c SAXS scattering data of TRF1TRFH, TERB2N-TERB1TRFB, TRF1TRFH-TERB1TRFB and TRF1TRFH-TERB1TRFB-TERB2N overlaid with the theoretical scattering curves of their modelled structures (red; χ2 values of 1.70, 1.42, 1.43 and 1.02, respectively). The scattering data points below the minimum Q-value of the Guinier analysis are shown in grey. d Multi-phase SAXS model of TRF1TRFH-TERB1TRFB-TERB2N in which TRF1TRFH is shown in green with its known crystal structure superposed (PDB accession 5WIR45), and TERB1TRFB and TERB2N are shown in red and blue, respectively. e Model of the 2:1:1 TRF1–TERB1–TERB2 complex. The dimeric cleft of the TRF1 TRFH domains interacts with TERB1 through the TRFB region that includes its binding site for the globular N-terminus of TERB2.
