4.8 Article

The quantitative and condition-dependent Escherichia coli proteome

Journal

NATURE BIOTECHNOLOGY
Volume 34, Issue 1, Pages 104-110

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/nbt.3418

Keywords

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Funding

  1. Netherlands Organisation for Scientific Research (NWO) (VIDI grant) [864.11.001]
  2. Dupont (Dupont Young Professorship Award)
  3. Swiss National Science Foundation [31003A_132428/1]
  4. Commission of the European Communities through the PROSPECTS consortium (EU FP7 project) [201648]
  5. PROMYS consortium (EU H2020 project) [613745]
  6. Marie Curie Intra-European Fellowship (IEF) [330150]
  7. 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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