Background: Escherichia coli is a well-studied anaerobic bacteria which is able to regulate metabolic pathways depending on the type of sugar presented in the medium. We have studied the glucose-lactose shift in E. coli at the protein level using a recently developed mass spectrometry platform.
Method: Cells were grown in minimal medium containing two sugars (glucose and lactose) and analyzed using novel mass spectrometry cluster. The cluster combines the high resolving power and dynamic range of Fourier transform ion cyclotron resonance (FTICR) for accurate mass measurement and quantitation with multiple ion traps for fast and sensitive tandem mass spectrometry. The protein expression profile was followed in time across the glucose-lactose diauxic shift using label-free quantitation from the FTICR data.
Results and conclusion: The entire dataset was interrogated by KEGG pathway analysis, mapping measured changes in protein abundance onto known metabolic pathways. The obtained results were consistent with previously published gene expression data, with β-galactosidase being the most strongly induced protein during the diauxic shift.