The quantitative and condition-dependent Escherichia coli proteomeSchmidt, A., Kochanowski, K., Vedelaar, S., Ahrné, E., Volkmer, B., Callipo, L., Knoops, K., Bauer, M., Aebersold, R. & Heinemann, M., Jan-2016, In : Nature Biotechnology. 34, 1, p. 104-110 7 p.
Research output: Contribution to journal › Article › Academic › peer-review
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.
|Number of pages||7|
|Early online date||7-Dec-2015|
|Publication status||Published - Jan-2016|
- MASS-SPECTROMETRY, EVOLUTIONARY CONSERVATION, GENE-EXPRESSION, COG DATABASE, GROWTH-RATE, B-R, ACETYLATION, PROTEINS, REVEALS, RATES
Schmidt, A. (Creator), Kochanowski, K. (Creator), Bonsing-Vedelaar, S. (Creator), Ahrne, E. (Creator), Volkmer, B. (Creator), Callipo, L. (Creator), Knoops, K. (Creator), Bauer, M. (Creator), Aebersold, R. (Creator), Heinemann, M. (Creator), European Bioinformatics Institute (EMBL-EBI), 2015