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Originally published In Press as doi:10.1074/mcp.D500006-MCP200 on May 19, 2005.
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Molecular & Cellular Proteomics 4:1205-1209, 2005.
© 2005 by The American Society for Biochemistry and Molecular Biology, Inc.

Dataset

Localization, Annotation, and Comparison of the Escherichia coli K-12 Proteome under Two States of Growth*,S

Ana Lopez-Campistrous{ddagger}, Paul Semchuk{ddagger}, Lorne Burke{ddagger}, Taunja Palmer-Stone{ddagger}, Stephen J. Brokx§, Gordon Broderick{ddagger}, Drell Bottorff{ddagger}, Sandra Bolch{ddagger}, Joel H. Weiner{ddagger},§,¶ and Michael J. Ellison{ddagger},§,||

From the {ddagger} Institute for Biomolecular Design, 3-55 Medical Sciences Building and the § Department of Biochemistry, 4-74 Medical Sciences Building, University of Alberta, Edmonton, Alberta T6G 2H7, Canada

Here we describe a proteomic analysis of Escherichia coli in which 3,199 protein forms were detected, and of those 2,160 were annotated and assigned to the cytosol, periplasm, inner membrane, and outer membrane by biochemical fractionation followed by two-dimensional gel electrophoresis and tandem mass spectrometry. Represented within this inventory were unique and modified forms corresponding to 575 different ORFs that included 151 proteins whose existence had been predicted from hypothetical ORFs, 76 proteins of completely unknown function, and 222 proteins currently without location assignments in the Swiss-Prot Database. Of the 575 unique proteins identified, 42% were found to exist in multiple forms. Using DIGE, we also examined the relative changes in protein expression when cells were grown in the presence and absence of amino acids. A total of 23 different proteins were identified whose abundance changed significantly between the two conditions. Most of these changes were found to be associated with proteins involved in carbon and amino acid metabolism, transport, and chemotaxis. Detailed information related to all 2,160 protein forms (protein and gene names, accession numbers, subcellular locations, relative abundances, sequence coverage, molecular masses, and isoelectric points) can be obtained upon request in either tabular form or as interactive gel images.

|| To whom correspondence should be addressed: Inst. for Biomolecular Design, 3-67 Medical Sciences Bldg., University of Alberta, Edmonton, Alberta T6G 2H7, Canada. Tel.: 780-492-6352; Fax: 780-492-9394; E-mail: mike.ellison{at}ualberta.ca


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