The quantitative and condition-dependent Escherichia coli proteome

被引：526

作者：

Schmidt, Alexander ^{[1
]}

Kochanowski, Karl ^{[2
]}

Vedelaar, Silke ^{[3
]}

Ahrne, Erik ^{[1
]}

Volkmer, Benjamin ^{[2
]}

Callipo, Luciano ^{[2
]}

Knoops, Kevin ^{[4
]}

Bauer, Manuel ^{[1
]}

Aebersold, Ruedi ^{[2
,5
]}

Heinemann, Matthias ^{[2
,3
]}

机构：

[1] Univ Basel, Biozentrum, Basel, Switzerland

[2] Swiss Fed Inst Technol, Inst Mol Syst Biol, Zurich, Switzerland

[3] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Mol Syst Biol, Groningen, Netherlands

[4] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Mol Cell Biol, Groningen, Netherlands

[5] Univ Zurich, Fac Sci, Zurich, Switzerland

来源：

NATURE BIOTECHNOLOGY | 2016年 / 34卷 / 01期

基金：

瑞士国家科学基金会; 欧洲研究理事会; 欧盟地平线“2020”;

关键词：

EVOLUTIONARY CONSERVATION; GROWTH; ACETYLATION; PROTEINS; REVEALS; PHOSPHOPROTEOME; QUANTIFICATION; IDENTIFICATION; COVERAGE; DATABASE;

D O I：

10.1038/nbt.3418

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

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.

引用

页码：104 / 110

页数：7

共 51 条

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