1. Structure and dynamics of UBA5-UFM1 complex formation showing new insights in the UBA5 activation mechanism.
- Author
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Fuchs S, Kikhney AG, Schubert R, Kaiser C, Liebau E, Svergun DI, Betzel C, and Perbandt M
- Subjects
- Humans, Models, Molecular, Multiprotein Complexes metabolism, Protein Binding, Proteins genetics, Proteins metabolism, Scattering, Small Angle, Spectrometry, Fluorescence, Ubiquitin-Activating Enzymes genetics, Ubiquitin-Activating Enzymes metabolism, X-Ray Diffraction, Molecular Dynamics Simulation, Multiprotein Complexes chemistry, Protein Conformation, Protein Multimerization, Proteins chemistry, Ubiquitin-Activating Enzymes chemistry
- Abstract
Ubiquitin fold modifier 1 (UFM1) is an ubiquitin-like protein (Ubl) involved especially in endoplasmic stress response. Activation occurs via a three-step mechanism like other Ubls. Data obtained reveal that UFM1 regulates the oligomeric state of ubiquitin activating enzyme 5 (UBA5) to initiate the activation step. Mixtures of homodimers and heterotrimers are observed in solution at the equilibrium state, demonstrating that the UBA5-UFM1 complex undergoes several concentration dependent oligomeric translational states to form a final functional complex. The oligomerization state of unbound UBA5 is also concentration dependent and shifts from the monomeric to the dimeric state. Data describing different oligomeric states are complemented with binding studies that reveal a negative cooperativity for the complex formation and thereby provide more detailed insights into the complex formation mechanism., (Copyright © 2021 Elsevier Inc. All rights reserved.)
- Published
- 2021
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