Fig. 5: Functional characterization of PML CC domain.
From: Cryo-EM structure of PML RBCC dimer reveals CC-mediated octopus-like nuclear body assembly mechanism
a Three hydrophobic pockets were observed in PML CC dimer. PML1 and PML2 were shown in cartoon representation and colored in blue and green, respectively. Hydrophobic residues in the hydrophobic pockets were annotated and shown in stick representation. b Size-exclusion analytical chromatography of the purified PML46−256, PML46−287, PML46−323, PML46−362, and PML46−391. The calibrated molecular weights of each elution/fraction were shown above the chromatographic traces. The N-termini of the aforementioned truncation mutants were all fused with an MBP tag. c Fluorescence visualization of HeLaPml−/− cells expressing EGFP-PML, EGFP-PMLL240R, EGFP-PMLL247R, and EGFP-PMLI279R. Scale bar, 5 µm. Statistical analysis of PML NB formation was conducted. All experiments were performed in independent replicates, with NB counts calculated from ≥ 15 nuclei. Data are means ± SEM. ****P < 0.0001 (derived from ordinary one-way ANOVA test). All experiments/results displayed in the main figure were conducted with PML isoform IV.
