Protein expression dynamics during Escherichia Coli glucose-lactose diauxie

BMC Microbiology

Research Article

Magnus Palmblad¹  André M Deelder¹  Ekaterina Mostovenko¹ 

[1] Department of Parasitology, Biomolecular Mass Spectrometry Unit, Leiden University Medical Center, P.O. Box 9600, Zone L04-Q, 2300 RC, Leiden, Netherlands;

关键词: label-free;    quantitative mass spectrometry;    β-galactosidase;    Escherichia coli;    glucose-lactose diauxie;   

DOI  :  10.1186/1471-2180-11-126

 received in 2010-12-10, accepted in 2011-06-01,  发布年份 2011

来源: Springer

【 摘 要 】

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.

【 授权许可】

CC BY   
© Mostovenko et al; licensee BioMed Central Ltd. 2011