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Non-linear Min protein interactions generate harmonics that signal mid-cell division in Escherichia coli

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  • James C Walsh
  • Christopher N Angstmann
  • Iain G Duggin
  • Paul M G Curmi

Abstract

The Min protein system creates a dynamic spatial pattern in Escherichia coli cells where the proteins MinD and MinE oscillate from pole to pole. MinD positions MinC, an inhibitor of FtsZ ring formation, contributing to the mid-cell localization of cell division. In this paper, Fourier analysis is used to decompose experimental and model MinD spatial distributions into time-dependent harmonic components. In both experiment and model, the second harmonic component is responsible for producing a mid-cell minimum in MinD concentration. The features of this harmonic are robust in both experiment and model. Fourier analysis reveals a close correspondence between the time-dependent behaviour of the harmonic components in the experimental data and model. Given this, each molecular species in the model was analysed individually. This analysis revealed that membrane-bound MinD dimer shows the mid-cell minimum with the highest contrast when averaged over time, carrying the strongest signal for positioning the cell division ring. This concurs with previous data showing that the MinD dimer binds to MinC inhibiting FtsZ ring formation. These results show that non-linear interactions of Min proteins are essential for producing the mid-cell positioning signal via the generation of second-order harmonic components in the time-dependent spatial protein distribution.

Suggested Citation

  • James C Walsh & Christopher N Angstmann & Iain G Duggin & Paul M G Curmi, 2017. "Non-linear Min protein interactions generate harmonics that signal mid-cell division in Escherichia coli," PLOS ONE, Public Library of Science, vol. 12(10), pages 1-16, October.
  • Handle: RePEc:plo:pone00:0185947
    DOI: 10.1371/journal.pone.0185947
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    References listed on IDEAS

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    1. Debnath Ghosal & Daniel Trambaiolo & Linda A. Amos & Jan Löwe, 2014. "MinCD cell division proteins form alternating copolymeric cytomotive filaments," Nature Communications, Nature, vol. 5(1), pages 1-11, December.
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