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February 16, 2016Proceedings of the National Academy of Sciences141 citationsOpen Access

Membrane-bound MinDE complex acts as a toggle switch that drives Min oscillation coupled to cytoplasmic depletion of MinD

AVAnthony G. VecchiarelliMLMin LiMMMichiyo Mizuuchi

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Abstract

The Escherichia coli Min system self-organizes into a cell-pole to cell-pole oscillator on the membrane to prevent divisions at the cell poles. Reconstituting the Min system on a lipid bilayer has contributed to elucidating the oscillatory mechanism. However, previous in vitro patterns were attained with protein densities on the bilayer far in excess of those in vivo and failed to recapitulate the standing wave oscillations observed in vivo. Here we studied Min protein patterning at limiting MinD concentrations reflecting the in vivo conditions. We identified "burst" patterns--radially expanding and imploding binding zones of MinD, accompanied by a peripheral ring of MinE. Bursts share several features with the in vivo dynamics of the Min system including standing wave oscillations. Our data support a patterning mechanism whereby the MinD-to-MinE ratio on the membrane acts as a toggle switch: recruiting and stabilizing MinD on the membrane when the ratio is high and releasing MinD from the membrane when the ratio is low. Coupling this toggle switch behavior with MinD depletion from the cytoplasm drives a self-organized standing wave oscillator.

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Cite This Study

Vecchiarelli et al. (2016) studied this question.

synapsesocial.com/papers/6a20f9ebca0ee60525c6ca16https://doi.org/10.1073/pnas.1600644113
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Also Consider

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  1. 1Differential affinities of MinD and MinE to anionic phospholipid influence Min patterning dynamics in vitro2014 · 108 citations
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  5. 5A conserved sequence at the C‐terminus of MinD is required for binding to the membrane and targeting MinC to the septum2003 · 213 citations