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. 2017 Aug 30;114(38):E7949–E7958. doi: 10.1073/pnas.1711158114

Fig. S7.

Fig. S7.

The UAB motif harbors features for interaction with H2AK119ub nucleosomes. (A) Sequence alignment of the UAB motif across species. Conserved amino acids are heighted in black or gray. The arginine residues likely involved in binding to the nucleosome acidic patch are marked with asterisks. The two clusters of conserved aliphatic residues potentially binding to the ubiquitin hydrophobic patch are indicated by bracket. (B) A structural modeling of the UAB motif complexed with H2AK119ub nucleosome. The UAB motif is shown in pink. The electrostatic potential of nucleosome core octamer is shown, where blue stands for positive charge and red for negative charge. The side chains of the residues in the ubiquitin hydrophobic patch are shown in spheres, and H2A/H2B ubiquitination sites are indicated with arrows. The distance of the acidic patch to H2BK120 is shorter than that to H2AK119, indicating that the spacing between arginine fingers and aliphatic clusters is important for the preferred binding to H2AK119ub nucleosomes.