Profiling of the E. coli cytoplasmic membrane proteome: biogenesis, turnover, organization and function

Project leader

Funding source

Swedish Research Council - Vetenskapsrådet (VR)

Project Details

Start date: 01/01/2007
End date: 31/12/2009
Funding: 2400000 SEK


Integral membrane proteins account for 20-30% of all open reading frames in sequenced pro- and eukaryotic genomes, and they fulfill a wide range of central functions in the cell. However, our knowledge of this important class of proteins is still poor. The goal of my laboratory is to provide the first comprehensive overview of the biogenesis, turnover, organization and function of a membrane proteome. As a model system, we use the cytoplasmic membrane proteome of the bacterium Escherichia coli. This bacterium is the ideal platform for the global analysis of a membrane proteome since its complete genome has been sequenced and it is readily amenable to both genetic manipulation and membrane protein biochemistry. In our studies we use a combination of state-of-the-art techniques; e.g., flow cytometry, 1/2D-gelelectrophoresis techniques, mass spectrometry, bioinformatics and a by our own lab developed Green fluorescent protein (GFP)-based pipeline for the overexpression and isolation of membrane proteins. Importantly, the cytoplasmic membrane of E. coli contains a diverse array of biochemical functions, many of which are analogous to those found in more specialized membranes in eukaryotic organisms and pathogenic bacteria. Finally, the global analysis of the cytoplasmic membrane proteome of E. coli will result in the development of much needed large-scale methodologies and strategies for membrane protein research and serve as an important reference for other membrane proteomes.

Last updated on 2017-31-03 at 12:58