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Mol Microbiol. 2007 Jun;64(6):1419-22.

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

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1
Department of Biochemistry and Molecular Biology, University of Texas--Houston Medical School, Houston, TX 77225, USA. Eugenia.Mileykovskaya@uth.tmc.edu

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.

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