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Charge-Patterned Disordered Peptides Tune Intracellular Phase Separation in Bacteria.

Jane Liao1, Vivian Yeong1, Allie C Obermeyer1

  • 1Department of Chemical Engineering, Columbia University, New York, New York 10027, United States.

ACS Synthetic Biology
|February 3, 2024
PubMed
Summary

Scientists engineered bacterial protein condensates using electrostatic interactions. Modifying protein charge distribution with disordered peptides controlled condensate size, number, and location in E. coli.

Keywords:
biomolecular condensatecomplex coacervationmembraneless organelleprotein phase separation

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Area of Science:

  • Cell Biology
  • Biophysics
  • Molecular Biology

Background:

  • Subcellular phase-separated compartments, or biomolecular condensates, are crucial for cellular organization.
  • Understanding the sequence-specific drivers of phase separation in bacteria is essential.

Purpose of the Study:

  • To investigate sequence determinants of protein phase separation in bacteria.
  • To engineer controllable protein-based condensates in *Escherichia coli*.

Main Methods:

  • Utilized electrostatic interactions as the primary driving force for phase separation.
  • Engineered minimal cationic disordered peptides to modify model proteins (negative, neutral, positive).
  • Investigated the impact of protein charge distribution and peptide characteristics on condensate formation and properties.

Main Results:

  • Engineered protein condensates in *E. coli* by enhancing electrostatic interactions.
  • Phase behavior was modulated by interaction strength (dependent on net charge and charge distribution) and protein concentration.
  • Protein charge distribution between globular and disordered domains tuned condensate mesoscale attributes (size, number, localization).
  • Disordered peptide length and charge density affected protein expression and condensate formation.

Conclusions:

  • Charge-patterned disordered peptides offer a tunable platform for engineering bacterial biomolecular condensates.
  • This approach provides insights into the molecular grammar governing phase separation in bacteria.
  • Demonstrated control over condensate formation and properties through protein design.