Subcellular localization of Escherichia coli osmosensory transporter ProP: focus on cardiolipin membrane domains

Abstract

The role for specific lipids in the spatial distribution of the membrane proteins and formation of the lipid-protein membrane domains is an emerging theme in the studies of the supramolecular organization of the bacterial cell. A combination of the lipid and protein visualization techniques with manipulation of the cell lipid composition provides a useful tool for these studies. This MicroCommentary reviews the first experimental example demonstrating an involvement of the phospholipid cardiolipin in recruitment of a membrane protein (specifically H(+)-osmoprotectant symporter ProP) to the Escherichia coli cell poles. The properties of cardiolipin domains employed in creating a specific environment for structural organization and function of membrane protein complexes are also discussed.