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Slice Collision-Induced Unfolding and Molecular Dynamics Reveal How Post-Translational Succination Reshapes SUMO1
Louis Groignet1,2, Thomas Robert1, Quentin Duez1
1Organic Synthesis and Mass Spectrometry Laboratory, Department of Chemistry, Research Institute for Biosciences, University of Mons, Place du Parc 23, MonsB-7000, Belgium.
Small ubiquitin-like modifier 1 (SUMO1) succination alters its structure and stability. Advanced ion mobility spectrometry-mass spectrometry reveals modified unfolding due to new interactions in succinated SUMO1.
Area of Science:
- Biochemistry
- Proteomics
- Chemical Biology
Background:
- Small ubiquitin-like modifier 1 (SUMO1) is crucial for post-translational modifications.
- SUMO1 can undergo succination, a modification affecting its properties.
Purpose of the Study:
- To investigate structural and gas-phase stability changes in SUMO1 after succination.
- To elucidate the mechanisms behind these modifications at an atomistic level.
Main Methods:
- Ion mobility spectrometry-mass spectrometry (IMS-MS) techniques, including collision-induced unfolding (CIU) and slice-CIU.
- Molecular dynamics simulations.
Main Results:
- Succination of SUMO1 by diethyl fumarate induces significant structural and gas-phase stability alterations.
- CIU experiments demonstrated a modified unfolding pathway for succinated SUMO1.
- New charge-dipole interactions involving the succinyl moiety were identified.
Conclusions:
- Succination impacts SUMO1's structural dynamics and stability in the gas phase.
- IMS-MS and simulations provide atomistic insights into the effects of succination on SUMO1.
- Understanding these modifications is key to SUMOylation pathway research.
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