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

Halatek, Jacob and Frey, Erwin (2012): Highly Canalized MinD Transfer and MinE Sequestration Explain the Origin of Robust MinCDE-Protein Dynamics. In: Cell Reports, Vol. 1, No. 6: pp. 741-752

Abstract

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.

• Item Type: Journal article
• Form of publication: Publisher's Version
• Faculties: Physics
• Subjects: 500 Science > 530 Physics
• ISSN: 2211-1247
• Place of Publication: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA
• Language: English