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Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions
- Source :
- Nature Communications, Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
- Publication Year :
- 2021
- Publisher :
- Nature Publishing Group UK, 2021.
-
Abstract
- Liquid–liquid phase separation of proteins underpins the formation of membraneless compartments in living cells. Elucidating the molecular driving forces underlying protein phase transitions is therefore a key objective for understanding biological function and malfunction. Here we show that cellular proteins, which form condensates at low salt concentrations, including FUS, TDP-43, Brd4, Sox2, and Annexin A11, can reenter a phase-separated regime at high salt concentrations. By bringing together experiments and simulations, we demonstrate that this reentrant phase transition in the high-salt regime is driven by hydrophobic and non-ionic interactions, and is mechanistically distinct from the low-salt regime, where condensates are additionally stabilized by electrostatic forces. Our work thus sheds light on the cooperation of hydrophobic and non-ionic interactions as general driving forces in the condensation process, with important implications for aberrant function, druggability, and material properties of biomolecular condensates.<br />Elucidating the molecular driving forces underlying liquid–liquid phase separation is a key objective for understanding biological function and malfunction. Here the authors show that a wide range of cellular proteins, including FUS, TDP-43, Brd4, Sox2, and Annexin A11, which form condensates at low salt concentrations, can reenter a phase-separated regime at high salt concentrations.
- Subjects :
- 0301 basic medicine
Work (thermodynamics)
Phase transition
631/45/612
General Physics and Astronomy
Cell Cycle Proteins
01 natural sciences
Molecular dynamics
Phase (matter)
Static electricity
Sf9 Cells
631/57
Multidisciplinary
132
Chemistry
639/766/747
article
3. Good health
DNA-Binding Proteins
Chemical physics
9
Hydrophobic and Hydrophilic Interactions
631/57/2269
Biophysical chemistry
Annexins
Science
Static Electricity
Biophysics
Molecular Dynamics Simulation
Spodoptera
010402 general chemistry
Intrinsically disordered proteins
Phase Transition
General Biochemistry, Genetics and Molecular Biology
03 medical and health sciences
639/638/440/56
Animals
Humans
14/35
82/83
SOXB1 Transcription Factors
Proteins
General Chemistry
119/118
0104 chemical sciences
030104 developmental biology
14/63
RNA-Binding Protein FUS
119
Biological physics
Transcription Factors
Subjects
Details
- Database :
- OpenAIRE
- Journal :
- Nature Communications, Nature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
- Accession number :
- edsair.doi.dedup.....6e76508f1c7f77c9dfa6f04a1b46d6ff