The quantitative and condition-dependent Escherichia coli proteome

By A. Schmidt, K. Kochanowski, Silke R. Vedelaar, Erik Ahrné, Benjamin Volkmer, Luciano Callipo, K. Knoops, Manuel Bauer, R. Aebersold, Matthias Heinemann. Nature Biotechnology, 2015

729 citations recorded by the source corpus.

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.

Subfields: Genetics, Materials Chemistry, Spectroscopy

View Paper: https://www.semanticscholar.org/paper/deb9bd5c453437f31e72eea77884029780d1a042

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Citations in the corpus

• The world of protein acetylation. (2016, background): “coli, analyzing PTMs under different growth conditions, identified 31 proteins being Nt-acetylated [25].”
• The universally-conserved transcription factor RfaH is recruited to a hairpin structure of the non-template DNA strand (2018, background): “Activated RfaH remains bound to the transcription elongation complex (TEC) until termination (Belogurov et al., 2009), excluding NusG present in 100-fold excess (Schmidt et al., 2016).”