Subcellular localization of Escherichia coli osmosensory transporter ProP: focus on cardiolipin membrane domains.
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.
Mileykovskaya
Eugenia
E
Department of Biochemistry and Molecular Biology, University of Texas--Houston Medical School, Houston, TX 77225, USA. Eugenia.Mileykovskaya@uth.tmc.edu
D002308:Cardiolipins / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D016764:Cell Polarity; D004926:Escherichia coli / Q000378:metabolism / Q000648:ultrastructure*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D008856:Microscopy, Fluorescence; D027981:Symporters / Q000378:metabolism*
D002308:Cardiolipins; D029968:Escherichia coli Proteins; C079244:ProP protein, E coli; D027981:Symporters