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Condensates formed by prion-like low-complexity domains have small-world network structures and interfaces defined by
Mina Farag1, Samuel R Cohen1, Wade M Borcherds2
1Department of Biomedical Engineering and Center for Biomolecular Condensates, Washington University in St. Louis, St. Louis, MO, USA.
Nature Communications
|December 13, 2022
Summary
Biomolecular condensates, crucial for cell function, organize via phase transitions. This study reveals how prion-like low complexity domains (PLCDs) form structured networks within condensates, influencing their biochemical activity.
Area of Science:
- Biochemistry
- Biophysics
- Molecular Biology
Background:
- Biomolecular condensates are essential cellular structures formed by phase transitions.
- These condensates involve multivalent macromolecules with associative and segregative properties.
Purpose of the Study:
- To characterize the molecular and mesoscale structure of condensates formed by prion-like low complexity domains (PLCDs).
- To understand the role of sticker-and-spacer architectures in condensate formation and properties.
Main Methods:
- Computational modeling of intrinsically disordered proteins.
- Analysis of phase behavior, network topology, and molecular organization within simulated condensates.
Main Results:
- PLCDs form condensates with sticker-and-spacer architectures, driving associative interactions via reversible crosslinking.
- Simulations reproduce experimentally observed sequence-specific phase behaviors.
- Condensates exhibit small-world network topologies with inhomogeneous molecular organization and specific interfacial features.
Conclusions:
- Simple condensates composed of a single macromolecule type display complex internal organization.
- The structural features of PLCD condensates, including their interface properties, are crucial for their biochemical activity.
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