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BMC Microbiology

, 11:126

Microbial biochemistry, physiology and metabolism


BackgroundEscherichia 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.

MethodCells 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 ConclusionThe 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.

Keywordslabel-free quantitative mass spectrometry β-galactosidase Escherichia coli glucose-lactose diauxie Electronic supplementary materialThe online version of this article doi:10.1186-1471-2180-11-126 contains supplementary material, which is available to authorized users.

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Autor: Ekaterina Mostovenko - André M Deelder - Magnus Palmblad


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