Acetylation of SUMO1 Alters Interactions with the SIMs of PML and Daxx in a Protein-Specific Manner

Structure. 2020 Feb 4;28(2):157-168.e5. doi: 10.1016/j.str.2019.11.019. Epub 2019 Dec 23.


The interactions between SUMO proteins and SUMO-interacting motif (SIM) in nuclear bodies formed by the promyelocytic leukemia (PML) protein (PML-NBs) have been shown to be modulated by either phosphorylation of the SIMs or acetylation of SUMO proteins. However, little is known about how this occurs at the atomic level. In this work, we examined the role that acetylation of SUMO1 plays on its binding to the phosphorylated SIMs (phosphoSIMs) of PML and Daxx. Our results demonstrate that SUMO1 binding to the phosphoSIM of either PML or Daxx is dramatically reduced by acetylation at either K39 or K46. However, acetylation at K37 only impacts binding to Daxx. Structures of acetylated SUMO1 variants bound to the phosphoSIMs of PML and Daxx demonstrate that there is structural plasticity in SUMO-SIM interactions. The plasticity observed in these structures provides a robust mechanism for regulating SUMO-SIM interactions in PML-NBs using signaling generated post-translational modifications.

Keywords: BRET; Daxx; ITC; PML; PML nuclear bodies; SUMO; SUMO-interacting motif; acetylation; crystallography; phosphorylation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Acetylation
  • Binding Sites
  • Co-Repressor Proteins / chemistry*
  • Co-Repressor Proteins / metabolism*
  • Crystallography, X-Ray
  • HEK293 Cells
  • Humans
  • Lysine / metabolism
  • Models, Molecular
  • Molecular Chaperones / chemistry*
  • Molecular Chaperones / metabolism*
  • Mutation
  • Phosphorylation
  • Promyelocytic Leukemia Protein / chemistry*
  • Promyelocytic Leukemia Protein / metabolism*
  • Protein Binding
  • Protein Conformation
  • Protein Domains
  • Protein Folding
  • SUMO-1 Protein / chemistry*
  • SUMO-1 Protein / genetics
  • SUMO-1 Protein / metabolism*


  • Co-Repressor Proteins
  • DAXX protein, human
  • Molecular Chaperones
  • Promyelocytic Leukemia Protein
  • SUMO-1 Protein
  • SUMO1 protein, human
  • PML protein, human
  • Lysine