Mechanistic insights of the Min oscillator via cell-free reconstitution and imaging

Phys Biol. 2018 Mar 1;15(3):031001. doi: 10.1088/1478-3975/aa9e5e.


The MinD and MinE proteins of Escherichia coli self-organize into a standing-wave oscillator on the membrane to help align division at mid-cell. When unleashed from cellular confines, MinD and MinE form a spectrum of patterns on artificial bilayers-static amoebas, traveling waves, traveling mushrooms, and bursts with standing-wave dynamics. We recently focused our cell-free studies on bursts because their dynamics recapitulate many features of Min oscillation observed in vivo. The data unveiled a patterning mechanism largely governed by MinE regulation of MinD interaction with membrane. We proposed that the MinD to MinE ratio on the membrane acts as a toggle switch between MinE-stimulated recruitment and release of MinD from the membrane. In this review, we summarize cell-free data on the Min system and expand upon a molecular mechanism that provides a biochemical explanation as to how these two 'simple' proteins can form the remarkable spectrum of patterns.

Publication types

  • Research Support, N.I.H., Intramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adenosine Triphosphatases / physiology*
  • Biomechanical Phenomena
  • Cell Cycle Proteins / physiology*
  • Cell Membrane / physiology*
  • Escherichia coli / physiology*
  • Escherichia coli Proteins / physiology*


  • Cell Cycle Proteins
  • Escherichia coli Proteins
  • MinE protein, E coli
  • Adenosine Triphosphatases
  • MinD protein, E coli