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Nat Biotechnol. 2016 Jan;34(1):104-10. doi: 10.1038/nbt.3418. Epub 2015 Dec 7.

The quantitative and condition-dependent Escherichia coli proteome.

Author information

1
Biozentrum, University of Basel, Basel, Switzerland.
2
Institute of Molecular Systems Biology, ETH Zurich, Zurich, Switzerland.
3
Molecular Systems Biology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, the Netherlands.
4
Molecular Cell Biology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, the Netherlands.
5
Faculty of Science, University of Zurich, Zurich, Switzerland.

Abstract

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.

PMID:
26641532
PMCID:
PMC4888949
DOI:
10.1038/nbt.3418
[Indexed for MEDLINE]
Free PMC Article

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