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Highly Canalized MinD Transfer and MinE Sequestration Explain the Origin of Robust MinCDE-Protein Dynamics

Highly Canalized MinD Transfer and MinE Sequestration Explain the Origin of Robust MinCDE-Protein Dynamics

Physik - Open Access LMU - Teil 01/02 vor 14 Jahren

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Min-protein oscillations in Escherichia coli are characterized by
the remarkable robustness with which spatial patterns dynamically
adapt to variations of cell geometry. Moreover, adaption, and
therefore proper cell division, is independent of temperature.
These observations raise fundamental questions about the mechanisms
establishing robust Min oscillations, and about the role of spatial
cues, as they are at odds with present models. Here, we introduce a
robust model based on experimental data, consistently explaining
the mechanisms underlying pole-to-pole, striped, and circular
patterns, as well as the observed temperature dependence of the
oscillation period. Contrary to prior conjectures, the model
predicts that MinD and cardiolipin domains are not colocalized. The
transient sequestration of MinE and highly canalized transfer of
MinD between polar zones are the key mechanisms underlying
oscillations. MinD channeling enhances midcell localization and
facilitates stripe formation, revealing the potential optimization
process from which robust Min-oscillations originally arose.