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MinC/MinD copolymers are not required for Min function

Kyung-Tae Park1, Shishen Du1, Joe Lutkenhaus1

  • 1Department of Microbiology, Molecular Genetics and Immunology, University of Kansas Medical Center, Kansas City, KS, 66160, USA.

Molecular Microbiology
|August 14, 2015
PubMed

Insights

Bacterial cell division relies on Min proteins to position the Z ring correctly. This study shows MinC/MinD copolymer formation is not essential for spatial regulation, challenging previous models.

Area of Science:

  • Microbiology
  • Cell Biology
  • Biochemistry

Background:

  • Precise placement of the Z ring during cell division in Escherichia coli is regulated by the Min proteins (MinC, MinD, and MinE).
  • MinD activates MinC, an FtsZ inhibitor, by recruiting it to the membrane and Z ring.
  • MinE stimulates MinD's ATPase activity, creating oscillations that exclude MinC/MinD from midcell.

Purpose of the Study:

  • To investigate the role of MinC/MinD copolymer formation in the spatial regulation of the Z ring.
  • To determine if MinC/MinD copolymerization is a prerequisite for the inhibitory activity of MinC on FtsZ.

Main Methods:

  • Utilized MinD mutants defective in MinC binding to create heterodimers unable to form MinC/MinD copolymers.
  • Generated heterodimers using MinC mutants defective in MinD binding.
  • Assessed the activity and spatial regulatory function of these non-copolymerizing heterodimers.

Main Results:

  • Heterodimers formed from MinC or MinD mutants defective in binding were active.
  • These active heterodimers were capable of mediating spatial regulation of the Z ring.
  • Demonstrated that MinC/MinD copolymer formation is not required for Z ring spatial regulation.

Conclusions:

  • MinC/MinD copolymerization is not essential for the spatial control of cell division in E. coli.
  • Supports a model where membrane-anchored MinC/MinD complexes target the Z ring via FtsZ's C-terminus, leading to FtsZ filament disruption.

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