Robustness of the division symmetry in Escherichia coli and functional consequences of symmetry breaking

Phys Biol. 2014 Nov 10;11(6):066005. doi: 10.1088/1478-3975/11/6/066005.

Abstract

The morphological symmetry of the division process of Escherichia coli is well-known. Recent studies verified that, in optimal growth conditions, most divisions are symmetric, although there are exceptions. We investigate whether such morphological asymmetries in division introduce functional asymmetries between sister cells, and assess the robustness of the symmetry in division to mild chemical stresses and sub-optimal temperatures. First, we show that the difference in size between daughter cells at birth is positively correlated to the difference between the numbers of fluorescent protein complexes inherited from the parent cell. Next, we show that the degree of symmetry in division observed in optimal conditions is robust to mild acidic shift and to mild oxidative stress, but not to sub-optimal temperatures, in that the variance of the difference between the sizes of sister cells at birth is minimized at 37 °C. This increased variance affects the functionality of the cells in that, at sub-optimal temperatures, larger/smaller cells arising from asymmetric divisions exhibit faster/slower division times than the mean population division time, respectively. On the other hand, cells dividing faster do not do so at the cost of morphological symmetry in division. Finally we show that at suboptimal temperatures the mean distance between the nucleoids increases, explaining the increased variance in division. We conclude that the functionality of E. coli cells is not immune to morphological asymmetries at birth, and that the effectiveness of the mechanism responsible for ensuring the symmetry in division weakens at sub-optimal temperatures.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Division / physiology*
  • Escherichia coli / cytology*
  • Escherichia coli / drug effects
  • Escherichia coli / genetics
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism
  • Green Fluorescent Proteins / genetics
  • Hydrogen Peroxide / pharmacology
  • Kinetics
  • Microscopy, Confocal
  • Models, Biological*
  • Recombinant Fusion Proteins / genetics
  • Stress, Physiological*
  • Temperature
  • Time-Lapse Imaging

Substances

  • Escherichia coli Proteins
  • Recombinant Fusion Proteins
  • Green Fluorescent Proteins
  • Hydrogen Peroxide