Extended Data Fig. 6: The formation of the D3–D14–D53 complex is mediated by the D2 domain of D53.
From: Structural plasticity of D3–D14 ubiquitin ligase in strigolactone signalling
a, Pull-down assay using recombinant ASK1–D3, His–D14, and GST-tagged N domain (D53-N), D1 domain (D53-D1) or D2 domain of D53. b–d, Size-exclusion chromatography analyses of the interaction between: full-length GST–D53, D14–GR24 and ASK1–D3 (b), D14–GR24 and either ASK1–D3 or ASK1–D3(ΔCTH) (c), and D14–GR24 and D53-D2 with ASK1–D3(ΔCTH) (d). All gels were resolved by SDS–PAGE and analysed by western blot using anti-GST and anti-His antibodies (as indicated under a) or Coomassie blue staining (b–d). All experiments shown in a–d were repeated independently at least three times.
