Inner membrane proteome of E. coli Min mutant

In bacteria, proteins of the MinD/ParA superfamily are reported to partition DNA and protein complexes to designate subcellular location. Among them, the E. coli Min system is a prominent example to demonstrate that the protein function is spatially regulated by the dynamic subcellular localization and by the reversible membrane topology. It is curious that pole-to-pole oscillation of MinDE involves continuous cycles of protein attachment to and detachment from the membrane, an environment that is crowded with a variety of proteins of different functions. We therefore took a quantitative proteomic approach, the isobaric tags for relative and absolute quantitation (iTRAQ) method, to analyze the inner memrbane proteome of the wild-type and Min mutant strains, aiming at identifying membrane and memrbane associated proteins that are affected in the absence of the Min system. The study reveals a physiological adapation strategy that could be used to rescue the unproductive rounds of cell division. The study also suggests that partition of macromolecules by the MinD/ParA family of proteins may have broader roles in bacterial physiology.