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Driving forces of the complex formation between highly charged disordered proteins.

Aritra Chowdhury1, Alessandro Borgia1, Souradeep Ghosh2

  • 1Department of Biochemistry, University of Zurich, Zurich 8057, Switzerland.

Proceedings of the National Academy of Sciences of the United States of America
|October 5, 2023
PubMed
Summary

This study reveals that counterion release entropy drives interactions between oppositely charged intrinsically disordered proteins, like histone H1 and prothymosin α. Ternary complexes also contribute to the observed thermodynamics.

Keywords:
intrinsically disordered proteinspolyelectrolyte complexationprotein bindingsingle-molecule spectroscopy

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Area of Science:

  • Biochemistry
  • Biophysics
  • Molecular Biology

Background:

  • Intrinsically disordered proteins (IDPs) form highly disordered complexes.
  • Oppositely charged IDPs represent a novel class of biomolecular interactions.

Purpose of the Study:

  • Investigate the thermodynamic driving forces behind interactions between intrinsically disordered proteins.
  • Characterize the binding of histone H1 (H1) and prothymosin α (ProTα).

Main Methods:

  • Temperature-dependent single-molecule Förster resonance energy transfer (smFRET).
  • Isothermal titration calorimetry (ITC).
  • Salt-dependent affinity measurements.
  • Mean-field polyelectrolyte theory.

Main Results:

  • ProTα-H1 binding is enthalpically unfavorable.
  • Counterion release entropy is a key thermodynamic driver.
  • Ternary complexes of ProTα and H1 exist alongside heterodimers.
  • Observed thermodynamics are quantitatively explained by polyelectrolyte theory.

Conclusions:

  • Counterion release is crucial for charged biomolecular interactions.
  • ProTα-H1 complex formation principles apply broadly to charged biomolecules.
  • IDP complex formation shares similarities with synthetic polyelectrolyte interactions.