Impact of dramatic structural changes of MinE on the patterning of the E. coli Min protein system. — ASN Events

Impact of dramatic structural changes of MinE on the patterning of the E. coli Min protein system. (#171)

James C Walsh 1 2 , Iain Duggin 1 , Chris Angstmann 2 , Paul Curmi 2
  1. ithree institute, University of Technology, Sydney, NSW, Australia
  2. UNSW, NSW, Australia

Oscillations of the E. coli Min protein system are in part responsible for the correct placement of the cell division apparatus at mid-cell. The oscillations are spontaneously generated within the cell by the interactions and diffusion of the MinCDE proteins, which effectively create concentration gradients that inhibit assembly of the division protein FtsZ near the poles of the rod-shaped cell. There is experimental evidence for many non-linear effects of the Min system, such as cooperative membrane binding. This study utilises the known molecular interactions of the Min system to generate a model that accounts for the majority of properties of the Min protein system. This model autonomously reproduces the observed changes in spatiotemporal patterning of MinD as cells grow and divide. NMR and crystallography experiments have previously shown that a drastic change in the structure of MinE occurs between its active and inactive state.  Experiments also suggest the existence of several intermediary transitional states. Using our model for min oscillation, we probe the impact of different potential confirmations/activity of these states. Comparing resulting patterning to experimental kymographs, we propose a complete pathway for the transition of MinE between its active and inactive form.