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Interfacing bacterial microcompartment shell proteins with genetically encoded condensates.

Michele Costantino1, Eric J Young2,3, Abesh Banerjee1

  • 1School of Molecular Sciences, Arizona State University, Tempe, Arizona, USA.

Protein Science : a Publication of the Protein Society
|February 19, 2025
PubMed
Summary
This summary is machine-generated.

Bacterial microcompartment (BMC-H) shell proteins coat synthetic protein condensates, creating stable, controllable compartments. This advance offers a new method for engineering synthetic cells and organelles with tunable properties.

Keywords:
bacterial microcompartmentscompartmentalizationliquid–liquid phase separationself‐assemblysynthetic biology

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Area of Science:

  • Biochemistry
  • Synthetic Biology
  • Biophysics

Background:

  • Liquid-liquid phase separation (LLPS) drives the formation of cellular condensates, crucial for synthetic cell development.
  • Bacterial microcompartment (BMC) shell proteins are known for forming robust proteinaceous structures.

Purpose of the Study:

  • To investigate the assembly of BMC-H proteins on LLPS-driven protein condensates.
  • To engineer BMC-H variants for surface coating of condensates.
  • To evaluate the stability and functional properties of these coated condensates for synthetic biology applications.

Main Methods:

  • Utilized engineered protein condensates formed by tandem RGG-RGG domains.
  • Engineered BMC-H variants fused to RGG truncations to promote surface assembly.
  • Investigated pH and protein concentration effects on coating formation.
  • Assessed condensate coalescence, stability, and selective protein sequestration (e.g., TEV protease).

Main Results:

  • Engineered BMC-H variants, particularly BMC-H-T2, formed stable surface coatings on RGG-RGG droplets.
  • These coatings prevented droplet coalescence and were stable, not exchanging with the dilute phase.
  • Coated droplets selectively sequestered folded proteins like TEV protease.
  • TEV protease degraded the RGG-RGG core but not the BMC-H coating, demonstrating coating integrity.

Conclusions:

  • BMC shell protein-coated protein condensates are fully encodable and offer precise control over LLPS compartments.
  • This system provides a novel platform for building functional synthetic organelles and cells.
  • The ability to form stable, selective coatings opens avenues for advanced biomolecular engineering.