Fig. 1

JIL-1’s C-terminal domain interacts with JASPer’s LEDGF domain to form the JJ-complex. a Western blot analysis with α-JASPer and α-JIL-1 antibodies of co-IP from nuclear embryo extracts. Co-IP was performed with two different monoclonal α-JASPer antibodies containing culture supernatants and culture medium as control. The corresponding unbound fractions are loaded next to each IP. Molecular weight markers are shown to the left. Source data are provided as a Source Data file. b SDS-PAGE with Coomassie staining of recombinant JJ-complex purification from Sf21 cells using a baculovirus dual expression system of FLAG-JIL-1 and untagged JASPer. Molecular weight markers are shown to the left. A contaminant band is marked by asterisk. Source data are provided as a Source Data file. c JIL-1 and JASPer domain architecture drawn to scale. In JIL-1, PEST domains are highlighted in black, kinase domains in dark gray and a predicted prion-like domain in white. In JASPer, PWWP and LEDGF domains are highlighted in dark gray and conserved region in intermediate gray. C-terminal truncation breakpoints a–g for JIL-1 and N-terminal (N1-N3) and C-terminal truncation breakpoints (C1-C3) for JASPer used in d and e are indicated. Δ denotes the deletion in JASPer-ΔLEDGF. d Western blot analysis using α-JIL-1 and α-JASPer antibodies of co-IP experiments with extracts from Sf21 cells expressing wild type, untagged JASPer and various FLAG-JIL-1 C-terminal deletion mutants. Co-IP was performed with α-FLAG beads. Source data are provided as a Source Data file. e Western blot analysis as in d of co-IP experiments with extracts from Sf21 cells expressing various untagged JASPer deletion mutants and FLAG-JIL-1. Uninfected Sf21 cell extract was used as control (NV = no virus). Co-IP was performed with α-FLAG beads. Source data are provided as a Source Data file.