Bulk-surface coupling identifies the mechanistic connection between Min-protein patterns in vivo and in vitro

Self-organisation of Min proteins is responsible for the spatial control of cell division in Escherichia coli, and has been studied both in vivo and in vitro. Intriguingly, the protein patterns observed in these settings differ qualitatively and quantitatively. This puzzling dichotomy has not been resolved to date. Using reconstituted proteins in laterally wide microchambers with a well-controlled height, we experimentally show that the Min protein dynamics on the membrane crucially depend on the micro chamber height due to bulk concentration gradients orthogonal to the membrane. A theoretical analysis shows that in vitro patterns at low microchamber height are driven by the same lateral oscillation mode as pole-to-pole oscillations in vivo. At larger microchamber height, additional vertical oscillation modes set in, marking the transition to a qualitatively different in vitro regime. Our work reveals the qualitatively different mechanisms of mass transport that govern Min protein-patterns for different bulk heights and thus shows that Min patterns in cells are governed by a different mechanism than those in vitro. Self-organisation of Min protein patterns observed in vivo and in vitro differ qualitatively and quantitatively. Here the authors reconstituted Min proteins in laterally wide microchambers with a well-controlled height and show that the Min protein dynamics on the membrane crucially depend on the micro chamber height.

Automated summary

The self-organisation of Min protein patterns observed in vivo and in vitro differ qualitatively and quantitatively. This study reveals that the Min protein dynamics on the membrane crucially depend on the micro chamber height, with low heights showing similarity to pole-to-pole oscillations in vivo and larger heights exhibiting vertical oscillation modes in a qualitatively different in vitro regime.