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  The proteome landscape of the kingdoms of life

Müller, J. B., Geyer, P. E., Colaco, A. R., Treit, P. V., Strauss, M. T., Oroshi, M., et al. (2020). The proteome landscape of the kingdoms of life. NATURE, 582, 592-596. doi:10.1038/s41586-020-2402-x.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0006-A38E-2 Version Permalink: http://hdl.handle.net/21.11116/0000-0006-A391-D
Genre: Journal Article

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 Creators:
Müller, Johannes B.1, Author              
Geyer, Philipp E.1, Author              
Colaco, Ana R.2, Author
Treit, Peter V.1, Author              
Strauss, Maximilian T.1, Author              
Oroshi, Mario1, Author              
Doll, Sophia1, Author              
Winter, Sebastian Virreira1, Author              
Bader, Jakob M.1, Author              
Koehler, Niklas2, Author
Theis, Fabian2, Author
Santos, Alberto2, Author
Mann, Matthias1, Author              
Affiliations:
1Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              
2external, ou_persistent22              

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Free keywords: QUANTIFICATION; REVEALS; DRAFT
 Abstract: Proteins carry out the vast majority of functions in all biological domains, but for technological reasons their large-scale investigation has lagged behind the study of genomes. Since the first essentially complete eukaryotic proteome was reported(1), advances in mass-spectrometry-based proteomics(2)have enabled increasingly comprehensive identification and quantification of the human proteome(3-6). However, there have been few comparisons across species(7,8), in stark contrast with genomics initiatives(9). Here we use an advanced proteomics workflow-in which the peptide separation step is performed by a microstructured and extremely reproducible chromatographic system-for the in-depth study of 100 taxonomically diverse organisms. With two million peptide and 340,000 stringent protein identifications obtained in a standardized manner, we double the number of proteins with solid experimental evidence known to the scientific community. The data also provide a large-scale case study for sequence-based machine learning, as we demonstrate by experimentally confirming the predicted properties of peptides fromBacteroides uniformis. Our results offer a comparative view of the functional organization of organisms across the entire evolutionary range. A remarkably high fraction of the total proteome mass in all kingdoms is dedicated to protein homeostasis and folding, highlighting the biological challenge of maintaining protein structure in all branches of life. Likewise, a universally high fraction is involved in supplying energy resources, although these pathways range from photosynthesis through iron sulfur metabolism to carbohydrate metabolism. Generally, however, proteins and proteomes are remarkably diverse between organisms, and they can readily be explored and functionally compared at www.proteomesoflife.org.

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Language(s): eng - English
 Dates: 2020
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000541024900009
DOI: 10.1038/s41586-020-2402-x
 Degree: -

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Title: NATURE
Source Genre: Journal
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Publ. Info: MACMILLAN BUILDING, 4 CRINAN ST, LONDON N1 9XW, ENGLAND : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 582 Sequence Number: - Start / End Page: 592 - 596 Identifier: ISSN: 0028-0836