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Adenosine Triphosphate Mediates Phase Separation of Disordered Basic Proteins by Bridging Intermolecular Interaction
Divya Kota1, Ramesh Prasad1, Huan-Xiang Zhou1,2
1Department of Chemistry, University of Illinois Chicago, Chicago, Illinois 60607, United States.
Journal of the American Chemical Society
|January 4, 2024
Summary
Adenosine triphosphate (ATP) drives the formation of liquid-like protein droplets by acting as molecular bridges. These condensates exhibit rapid fusion and significant shear thinning due to dynamic ATP interactions.
Area of Science:
- Biochemistry
- Molecular Biology
- Biophysics
Background:
- Adenosine triphosphate (ATP) is vital for cellular energy and nucleic acid synthesis.
- Intrinsically disordered proteins (IDPs) play roles in cellular processes.
- Phase separation is a key mechanism for organizing cellular components.
Purpose of the Study:
- To investigate the role of ATP in the phase separation of basic intrinsically disordered proteins (bIDPs).
- To characterize the physical properties and dynamics of ATP-mediated bIDP condensates.
Main Methods:
- In vitro phase separation assays.
- Confocal microscopy for visualizing condensates.
- Rheological measurements to determine viscosity and interfacial tension.
- Analysis of ATP concentration effects on bIDP behavior.
Main Results:
- ATP mediates the formation of liquid-like condensates from bIDPs.
- ATP concentrates within these droplets, acting as bridges between protein chains.
- Condensates display low interfacial tension, high zero-shear viscosity, and rapid fusion.
- Extreme shear thinning is observed, attributed to rapid reformation of ATP bridges.
- High ATP concentrations lead to aggregation and fibril formation, not dissolution.
Conclusions:
- ATP is a critical regulator of bIDP phase separation and condensate properties.
- The ATP-bridged network governs the unique rheological behavior of these condensates.
- ATP concentration is a key factor determining the outcome of bIDP-ATP interactions, from liquid droplets to aggregates.
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