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Sequence Tendency for the Interaction between Low-Complexity Intrinsically Disordered Proteins.

Moxin Zhang1, Bin Xue2, Qingtai Li2

  • 1Zhejiang Province Key Laboratory of Quantum Technology and Device, School of Physics, Zhejiang University, Hangzhou310058, China.

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Summary
This summary is machine-generated.

Intrinsically disordered proteins (IDPs) drive liquid-liquid phase separation (LLPS) through transient interactions. A specific C-terminal region of the LAF-1 RGG domain mediates sustained associations, crucial for LLPS.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Reversible interactions of intrinsically disordered proteins (IDPs) drive liquid-liquid phase separation (LLPS).
  • The mechanisms of transient IDP interactions, including sequence features and conformational dynamics, remain poorly understood.
  • Understanding IDP interactions is key to elucidating the principles of LLPS.

Purpose of the Study:

  • To investigate the reversible association mechanisms of the LAF-1 RGG domain, an IDP with a very low LLPS concentration.
  • To explore the relationship between IDP conformational fluctuations, sequence features, and interaction behavior.
  • To identify specific regions within IDPs that mediate sustained interactions and contribute to LLPS.

Main Methods:

  • Atomistic molecular dynamics (MD) simulations were employed to study the reversible association of the LAF-1 RGG domain.
  • Analysis focused on the duration and nature of inter-domain associations.
  • Sequence features and conformational dynamics were correlated with interaction patterns.

Main Results:

  • The duration of RGG domain associations is highly heterogeneous, with sustained associations being dominant.
  • A specific C-terminal region (residues 138-168) was identified as a 'contact-prone region' mediating these sustained interactions.
  • Extended conformations during inherent fluctuations of the RGG domain are linked to the formation of this contact-prone region.

Conclusions:

  • A specific region within the LAF-1 RGG domain significantly dominates its interactions and is critical for LLPS.
  • Inherent conformational fluctuations are essential for the emergence of these interaction 'hot spots'.
  • Experimental validation confirmed the importance of this region for LLPS, highlighting the interplay between dynamics, sequence, and phase separation.