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ATP promotes protein coacervation through conformational compaction.

Yueling Zhu1,2, Shiyan Lin3, Lingshen Meng4

  • 1State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, Innovation Academy for Precision Measurement Science and Technology, Chinese Academy of Sciences, Wuhan 430071, China.

Journal of Molecular Cell Biology
|October 2, 2024
PubMed
Summary
This summary is machine-generated.

Adenosine triphosphate (ATP) concentration affects intrinsically disordered protein (IDP) phase separation in a biphasic manner. Low ATP promotes, while high ATP dissolves, IDP droplets through distinct molecular interactions.

Keywords:
ATPHNRNPGconformational compactionintrinsically disordered proteinphase separation

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Chemistry

Background:

  • Adenosine triphosphate (ATP) is known to act as a hydrotrope influencing protein phase separation.
  • Intrinsically disordered proteins (IDPs) undergo liquid-liquid phase separation (LLPS), a crucial process in cellular organization.
  • The role of ATP in modulating IDP phase separation, particularly its concentration-dependent effects, remains incompletely understood.

Purpose of the Study:

  • To investigate the biphasic effect of adenosine triphosphate (ATP) concentration on the phase separation of intrinsically disordered proteins (IDPs).
  • To elucidate the molecular mechanisms underlying ATP's dual role in promoting and inhibiting IDP phase separation.
  • To explore the impact of ATP on the structural conformation and intermolecular interactions of IDPs.

Main Methods:

  • Utilized the Arg-Gly/Arg-Gly-Gly (RG/RGG) rich motif from HNRNPG protein as a model IDP system.
  • Employed techniques to analyze protein phase separation, conformational changes, and intermolecular interactions under varying ATP concentrations.
  • Assessed solvent exchange rates and compression ratios during phase separation.

Main Results:

  • A biphasic relationship was observed between ATP concentration and IDP phase separation.
  • At low ATP concentrations, ATP neutralizes protein charges, enhances intermolecular interactions, and promotes phase separation, inducing a compact IDP conformation.
  • At high ATP concentrations, ATP's hydrotropic properties dominate, leading to the dissolution of phase-separated IDP droplets.

Conclusions:

  • ATP exhibits a complex, concentration-dependent modulation of IDP structure, interactions, and phase separation.
  • The findings reveal distinct mechanisms for ATP's influence at low (charge neutralization, interaction promotion) and high (hydrotropic dissolution) concentrations.
  • This study explains the differential phase separation behaviors of charge-rich RGG motifs compared to other low-complexity IDPs in the presence of ATP.