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The quantitative and condition-dependent Escherichia coli proteome

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.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Escherichia Coli

TISSUE(S): Permanent Cell Line Cell

SUBMITTER: Alexander Schmidt

LAB HEAD: Alexander Schmidt

PROVIDER: PXD000498 | Pride | 2015-10-12

REPOSITORIES: Pride

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The quantitative and condition-dependent Escherichia coli proteome.

Schmidt Alexander A Kochanowski Karl K Vedelaar Silke S Ahrné Erik E Volkmer Benjamin B Callipo Luciano L Knoops Kèvin K Bauer Manuel M Aebersold Ruedi R Heinemann Matthias M

Nature biotechnology 20151207 1

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-termina ...[more]

PMID: 26641532

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