The quantitative and condition-dependent Escherichia coli proteome

Alexander Schmidt*, Karl Kochanowski, Silke Vedelaar, Erik Ahrné, Benjamin Volkmer, Luciano Callipo, Kèvin Knoops, Manuel Bauer, Ruedi Aebersold, Matthias Heinemann

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

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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.

Original languageEnglish
Pages (from-to)104-110
Number of pages7
JournalNature Biotechnology
Volume34
Issue number1
Early online date7-Dec-2015
DOIs
Publication statusPublished - Jan-2016

Keywords

  • MASS-SPECTROMETRY
  • EVOLUTIONARY CONSERVATION
  • GENE-EXPRESSION
  • COG DATABASE
  • GROWTH-RATE
  • B-R
  • ACETYLATION
  • PROTEINS
  • REVEALS
  • RATES

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