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Depletion interactions modulate the binding between disordered proteins in crowded environments.

Franziska Zosel1, Andrea Soranno1,2, Karin J Buholzer3

  • 1Department of Biochemistry, University of Zurich, 8057 Zurich, Switzerland; franziska.zosel@gmail.com soranno@wustl.edu schuler@bioc.uzh.ch.

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Summary
This summary is machine-generated.

Macromolecular crowding affects intrinsically disordered protein (IDP) interactions. This study reveals crowding

Keywords:
intrinsically disordered proteinsmacromolecular crowdingsingle-molecule spectroscopy

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Intrinsically disordered proteins (IDPs) play crucial roles in cellular regulation.
  • IDP interactions are sensitive to environmental factors like salt concentration and posttranslational modifications.
  • The impact of macromolecular crowding on IDP interactions remains largely unexplored.

Purpose of the Study:

  • To investigate the influence of macromolecular crowding on the interaction between two IDPs that exhibit disorder-to-order transitions upon binding.
  • To quantify the effects of crowding on complex stability, binding kinetics, and microviscosity using single-molecule spectroscopy.

Main Methods:

  • Utilized single-molecule spectroscopy to simultaneously measure multiple interaction parameters.
  • Employed polyethylene glycol (PEG) as a crowding agent to mimic cellular macromolecular crowding.
  • Integrated experimental data with theoretical models of depletion interactions, considering the polymeric nature of IDPs and crowders.

Main Results:

  • Crowding significantly influences the equilibrium stability, association, and dissociation kinetics of the IDP complex.
  • A theoretical framework incorporating polymeric nature of IDPs and crowders quantitatively explains all observed effects.
  • The interaction enhancement by crowding is less pronounced for these IDPs compared to folded proteins of similar size.

Conclusions:

  • Macromolecular crowding impacts IDP interactions through depletion effects, modulated by the proteins' polymeric characteristics.
  • The developed integrated framework provides a coherent explanation for crowding effects on IDP complex formation.
  • Findings offer insights into the functional consequences of crowding on IDP-mediated cellular processes.