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Interfacial Assembly of Bacterial Microcompartment Shell Proteins in Aqueous Multiphase Systems.

A A Dharani T Abeysinghe1, Eric J Young2,3, Andrew T Rowland1

  • 1Department of Chemistry, Pennsylvania State University, State College, PA, 16801, USA.

Small (Weinheim an Der Bergstrasse, Germany)
|December 1, 2023
PubMed
Summary

Researchers combined bacterial microcompartment (BMC) shell proteins with liquid-liquid phase separation (LLPS) to create novel compartments. These protein-coated droplets offer a new strategy for synthetic cells, organizing biomimetic functions with cargo like enzymes or RNA.

Keywords:
bioreactorbottom‐up synthetic biologycompartmentalizationprotocellself‐assemblysynthetic cell

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Area of Science:

  • Biochemistry
  • Synthetic Biology
  • Materials Science

Background:

  • Compartmentalization is essential for life, achieved through various structures like lipid membranes, protein shells, or biopolymer phase separation.
  • Bacterial microcompartment (BMC) shell proteins are known for self-assembly, forming protein-based compartments within bacteria.
  • Liquid-liquid phase separation (LLPS) is a biophysical process creating membrane-less compartments through spontaneous de-mixing of cellular components.

Purpose of the Study:

  • To develop novel forms of compartmentalization by integrating BMC shell proteins with LLPS.
  • To investigate the assembly behavior of BMC proteins at liquid-liquid interfaces in different phase-separated systems.
  • To explore the potential of these engineered compartments for organizing biomimetic functionality within synthetic cells.

Main Methods:

  • Utilized poly(ethyleneglycol)/dextran aqueous two-phase systems and polylysine/polyaspartate complex coacervate systems to create liquid-liquid interfaces.
  • Assembled bacterial microcompartment (BMC) shell proteins at the interfaces of these phase-separated systems.
  • Investigated the influence of polyelectrolyte ratios and protein concentrations on interfacial assembly and competition with aggregation.
  • Developed a three-phase system by encapsulating coacervate droplets within dextran-rich droplets for tunable protein localization.

Main Results:

  • BMC shell proteins successfully assembled at the liquid-liquid interfaces of both PEG/dextran and coacervate systems.
  • Interfacial assembly in coacervate systems was sensitive to the ratio of cationic to anionic polypeptides, indicating electrostatic control.
  • Protein concentration and polycation availability influenced the competition between interfacial assembly and aggregation.
  • A three-phase system demonstrated tunable interfacial localization of BMC proteins by adjusting the polyelectrolyte charge ratio.

Conclusions:

  • BMC shell proteins can be directed to assemble at liquid-liquid interfaces, creating novel protein-coated droplets.
  • These engineered droplets, formed via LLPS and protein self-assembly, represent a new strategy for synthetic cell design.
  • The ability to encapsulate cargo like enzymes or RNA within these compartments enables the organization of biomimetic functions.