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The bacterial cell division regulators MinD and MinC form polymers in the presence of nucleotide

Joseph Conti1, Marissa G Viola1, Jodi L Camberg2

  • 1Department of Cell and Molecular Biology, The University of Rhode Island, Kingston, RI, USA.

FEBS Letters
|December 16, 2014
PubMed

Insights

The Min system, crucial for bacterial cell division, involves MinC, MinD, and MinE proteins. Researchers found MinD forms polymers with MinC and ATP, a process regulated by MinE.

Area of Science:

  • Cell Biology
  • Microbiology
  • Protein Biochemistry

Background:

  • The Min system (MinC, MinD, MinE) regulates cell division in Escherichia coli by forming polar gradients to position the septum.
  • MinC localization depends on MinD, a membrane-associated ATPase, while MinE modulates MinD's interaction with the membrane via ATP hydrolysis.

Purpose of the Study:

  • To investigate the polymerization of MinD and MinC proteins in vitro.
  • To elucidate the role of ATP and the MinE protein in the assembly and disassembly of MinCD complexes.
  • To characterize MinD mutants affecting polymerization.

Main Methods:

  • In vitro polymerization assays using purified MinC, MinD, and MinE proteins.
  • Biochemical analysis of protein-protein interactions and complex formation.
  • Characterization of MinD mutants (MinD(K11A) and MinD(ΔMTS15)) for polymerization defects.

Main Results:

  • MinD spontaneously forms polymers with MinC and ATP in the absence of phospholipids.
  • The topological regulator MinE induces the disassembly of these MinCD polymers.
  • Specific MinD mutations (K11A and ΔMTS15) abolish the ability of MinD to polymerize with MinC.

Conclusions:

  • MinD polymerization with MinC is an intrinsic property of the proteins, independent of membrane association.
  • MinE acts as a key regulator, promoting the disassembly of MinCD polymers.
  • The identified MinD mutants provide insights into the structural requirements for MinCD complex formation and bacterial cell division regulation.
Keywords:
ATPaseCytokinesisMin systemMinEPhospholipids

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