Fig. 2: PML monomer.
From: Cryo-EM structure of PML RBCC dimer reveals CC-mediated octopus-like nuclear body assembly mechanism
a Sequence alignment of the non-conserved region between the RING and B1 domains in human TRIM proteins. The α3 helix, which is unique to PML when compared with other TRIM proteins, was highlighted with dark green. b Interaction network of the α3 helix with the RING, B1, and B2 domains. α3 was depicted in dark green, RING in light green, B1 in tan, B2 in yellow green, and α6 in gray. c Fluorescence microscopy images of HeLaPml−/− cells expressing EGFP-PML, EGFP-PMLF108R, EGFP-PMLF109R, EGFP-PMLL112R, and EGFP-PMLL116E. 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 < 0.01, ****P < 0.0001 (derived from ordinary one-way ANOVA test). All experiments/results displayed in the main figure were conducted with PML isoform IV.
