A conserved sequence at the C-terminus of MinD is required for binding to the membrane and targeting MinC to the septum

Mol Microbiol. 2003 Jan;47(2):345-55. doi: 10.1046/j.1365-2958.2003.03321.x.


MinD is a key component of an oscillatory system that spatially regulates cell division in Escherichia coli. It is a peripheral membrane ATPase that recruits MinC and oscillates between the two halves of the cell in a MinE dependent manner. In vitro MinD binds to phospholipid vesicles in an ATP-dependent manner and is released through MinE-stimulated ATP hydrolysis. In this study we examined the function of the conserved C-terminus of MinD. Short truncations of three and ten amino acids dramatically decreased the ability of MinD to localize to the membrane and spatially regulate division. These truncations bound MinC but were deficient in targeting MinC to the septum. In vitro they dimerized, but were deficient in binding to phospholipid vesicles and undergoing MinE stimulation. We suggest a model in which the ATP-dependent dimerization of MinD affects the conformation of the C-terminal region, a potential amphipathic helix, triggering membrane binding.

MeSH terms

  • Adenosine Triphosphatases / chemistry*
  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / metabolism
  • Amino Acid Sequence
  • Cell Division
  • Cell Membrane / metabolism*
  • Conserved Sequence*
  • Dimerization
  • Escherichia coli / cytology*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism
  • Gene Deletion
  • Gene Expression Regulation, Bacterial*
  • Membrane Proteins / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Two-Hybrid System Techniques


  • Escherichia coli Proteins
  • Membrane Proteins
  • MinC protein, E coli
  • Adenosine Triphosphatases
  • MinD protein, E coli