Fig. 4

Interactions between Rif1 and other components in the PRC1.6 complex. A Schematic of the full-length and truncations of Rif1 proteins. B The LacO-LacI induced colocalization experiments reveal that both the N- and C-terminal regions of Rif1 can interact with Pcgf6. The full-length and truncations of Rif1 are shown in green, LacI-DsRed fused with Pcgf6 is shown in red, and DNA is stained with DAPI (blue). Bar: 10 μm. C The relative enrichment of GFP signals in the indicated experimental groups. **** p < 0.0001 by t-test, Error bars represent SD, n = 10–45 cells per group. D The LacO-LacI induced ectopic colocalization experiments reveal that Rif1 can interact with other components in the PRC1.6 complex. GFP-Rif1 is shown in green, LacI-DsRed fused with the indicated bait proteins are shown in red. DNA is stained with DAPI (blue). Bar: 10 μm. E The relative enrichment of GFP-Rif1 in the indicated experimental groups. **** p < 0.0001 by t-test, Error bars represent SD, n = 13–45 cells per group. F Coimmunoprecipitation of Pcgf6 and RNF2 with endogenous HA-Rif1. G-H Coimmunoprecipitations of Rif1 with endogenously HA-tagged Pcgf6 or Mga in mESCs