The quantitative and condition-dependent Escherichia coli proteome

A large-scale quantification of Escherichia coli proteomes across 22 experimental conditions. Measuring precise concentrations of proteins can provide insights into biological processes. Here we use efficient protein extraction and sample fractionation, as well as state-of-the-art quantitative mass...

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Veröffentlicht in:Nature biotechnology 2016-01, Vol.34 (1), p.104-110
Hauptverfasser: Schmidt, Alexander, Kochanowski, Karl, Vedelaar, Silke, Ahrné, Erik, Volkmer, Benjamin, Callipo, Luciano, Knoops, Kèvin, Bauer, Manuel, Aebersold, Ruedi, Heinemann, Matthias
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Sprache:eng
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Zusammenfassung:A large-scale quantification of Escherichia coli proteomes across 22 experimental conditions. Measuring precise concentrations of proteins can provide insights into biological processes. Here we use efficient protein extraction and sample fractionation, as well as state-of-the-art quantitative mass spectrometry techniques to generate a comprehensive, condition-dependent protein-abundance map for Escherichia coli . We measure cellular protein concentrations for 55% of predicted E. coli genes (>2,300 proteins) under 22 different experimental conditions and identify methylation and N-terminal protein acetylations previously not known to be prevalent in bacteria. We uncover system-wide proteome allocation, expression regulation and post-translational adaptations. These data provide a valuable resource for the systems biology and broader E. coli research communities.
ISSN:1087-0156
1546-1696
DOI:10.1038/nbt.3418