The quantitative and condition-dependent Escherichia coli proteome

A large-scale quantification of Escherichia coli proteomes across 22 experimental conditions. 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...

Full description

Saved in:
Bibliographic Details
Published in:Nature biotechnology 2016-01, Vol.34 (1), p.104-110
Main Authors: Schmidt, Alexander, Kochanowski, Karl, Vedelaar, Silke, Ahrné, Erik, Volkmer, Benjamin, Callipo, Luciano, Knoops, Kèvin, Bauer, Manuel, Aebersold, Ruedi, Heinemann, Matthias
Format: Article
Language:English
Subjects:
631/1647/2067
631/326/41/88
631/45/475
631/553/1833
82
82/58
Agriculture
Analysis
Bacteria
Bacterial proteins
Bioinformatics
Biomedical Engineering/Biotechnology
Biomedicine
Biotechnology
Cellular proteins
E coli
Escherichia coli
Escherichia coli - metabolism
Escherichia coli Proteins - metabolism
Fractionation
Genes
Life Sciences
Mass Spectrometry
Methylation
Physiological aspects
Proteins
Proteome
Proteomics
resource
Spectroscopy
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:A large-scale quantification of Escherichia coli proteomes across 22 experimental conditions. 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.
ISSN:1087-0156
1546-1696
DOI:10.1038/nbt.3418