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05:48
Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
Native structure protects SUMO proteins from aggregation into amyloid fibrils.
Raimon Sabate1, Alba Espargaro, Ricardo Graña-Montes
1Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, 08193 Bellaterra (Barcelona), Spain.
Biomacromolecules
|May 8, 2012
Summary
Small Ubiquitin-like Modifier (SUMO) proteins, crucial for cellular pathways, can unexpectedly aggregate into amyloid structures when their native state is disrupted. This aggregation risk highlights a conflict between protein function and folding stability.
Area of Science:
- Biochemistry
- Molecular Biology
- Structural Biology
Background:
- Small Ubiquitin-like Modifier (SUMO) proteins are essential in eukaryotes, involved in vital cellular processes.
- SUMO proteins are known for high solubility and regulating other proteins' solubility, relevant in neurodegenerative diseases.
- SUMOylation is critical, as pathway disruption is lethal in various organisms.
Purpose of the Study:
- To investigate the aggregation potential of human SUMO1, SUMO2, and SUMO3 proteins.
- To identify regions involved in SUMO aggregation and their relationship with functional interfaces.
Main Methods:
- Perturbation of native SUMO protein conformation.
- Analysis of aggregation into amyloid structures.
- Mapping of aggregation-mediating regions.
Main Results:
- Human SUMO1, SUMO2, and SUMO3 proteins can aggregate into amyloid structures upon perturbation.
- Aggregation is driven by specific regions that overlap with SUMO functional interfaces.
- A competition exists between SUMO protein function and aggregation propensity.
Conclusions:
- SUMO proteins, despite their native solubility, are susceptible to amyloid aggregation.
- Functional constraints may inherently create a trade-off between productive folding and aggregation in essential globular proteins.
- SUMO aggregation has potential physiological implications due to the critical nature of the SUMO pathway.
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