Journal
NATURE BIOTECHNOLOGY
Volume 34, Issue 1, Pages 104-110Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nbt.3418
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Funding
- Netherlands Organisation for Scientific Research (NWO) (VIDI grant) [864.11.001]
- Dupont (Dupont Young Professorship Award)
- Swiss National Science Foundation [31003A_132428/1]
- Commission of the European Communities through the PROSPECTS consortium (EU FP7 project) [201648]
- PROMYS consortium (EU H2020 project) [613745]
- Marie Curie Intra-European Fellowship (IEF) [330150]
- European Research Council [ERC-2008-AdG 233226]
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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.
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