ATP-Driven Separation of Liquid Phase Condensates in Bacteria

Mol Cell. 2020 Jul 16;79(2):293-303.e4. doi: 10.1016/j.molcel.2020.06.034.

Abstract

Liquid-liquid phase-separated (LLPS) states are key to compartmentalizing components in the absence of membranes; however, it is unclear whether LLPS condensates are actively and specifically organized in the subcellular space and by which mechanisms. Here, we address this question by focusing on the ParABS DNA segregation system, composed of a centromeric-like sequence (parS), a DNA-binding protein (ParB), and a motor (ParA). We show that parS and ParB associate to form nanometer-sized, round condensates. ParB molecules diffuse rapidly within the nucleoid volume but display confined motions when trapped inside ParB condensates. Single ParB molecules are able to rapidly diffuse between different condensates, and nucleation is strongly favored by parS. Notably, the ParA motor is required to prevent the fusion of ParB condensates. These results describe a novel active mechanism that splits, segregates, and localizes non-canonical LLPS condensates in the subcellular space.

Keywords: ParABS; liquid droplets; liquid phase condensation; phase separation; photo-activated localization microscopy; plasmid partition; single particle tracking.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / physiology*
  • Bacterial Physiological Phenomena*
  • DNA Primase / physiology
  • DNA, Bacterial
  • Escherichia coli Proteins / physiology*
  • Microscopy / methods
  • Nanoparticles
  • Phase Transition*
  • Single Molecule Imaging / methods

Substances

  • DNA, Bacterial
  • Escherichia coli Proteins
  • ParA protein, E coli
  • Adenosine Triphosphate
  • DNA Primase
  • dnaG protein, E coli