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Conformational and Interface Variability in Multivalent SIM-SUMO Interaction.

Alex Kötter1,2, Henning D Mootz3, Andreas Heuer1,2

  • 1Institut für Physikalische Chemie, Westfälische Wilhelms-Universität Münster, Corrensstraße 28/30, D-48149 Münster, Germany.

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SUMO targeted ubiquitin ligases (STUbLs) utilize multiple SUMO interacting motifs (SIMs) to bind SUMO chains. Molecular dynamics simulations reveal flexible STUbL-SUMO complexes with variable interfaces, challenging assumptions about restricted conformational freedom.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • SUMO targeted ubiquitin ligases (STUbLs) recognize SUMO chains via multiple SUMO interacting motifs (SIMs).
  • These SIMs are typically in disordered regions, and SUMO chains exhibit conformational flexibility.
  • Binding is assumed to significantly restrict SUMO chain movement.

Purpose of the Study:

  • To investigate the conformational dynamics of STUbL-SIM complexes using molecular dynamics simulations.
  • To analyze the interface interactions between RNF4's SIM2-SIM3 region and diSUMO3.
  • To compare simulation findings with experimental data.

Main Methods:

  • Extensive molecular dynamics simulations.
  • Analysis of SIM-SUMO interfaces.
  • Comparison with experimental data.

Main Results:

  • Simulations confirm the importance of canonical SIM-SUMO interfaces.
  • Non-canonical regions frequently mediate interactions.
  • The complex exhibits significant conformational flexibility due to variable interfaces.
  • Findings align with previous experimental measurements.

Conclusions:

  • STUbL-SUMO interactions are more conformationally flexible than previously assumed.
  • Variable binding interfaces contribute to this flexibility.
  • The findings are applicable to other multivalent SIM-SUMO complexes.