Selective identification of newly synthesized proteins in mammalian cells using bioorthogonal noncanonical amino acid tagging (BONCAT)
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In both normal and pathological states, cells respond rapidly to environmental cues by synthesizing new proteins. The selective identification of a newly synthesized proteome has been hindered by the basic fact that all proteins, new and old, share the same pool of amino acids and thus are chemically indistinguishable. We describe here a technology, based on the cotranslational introduction of azide groups into proteins and the chemoselective tagging of azide-labeled proteins with an alkyne affinity tag, to separate and identify, specifically, the newly synthesized proteins in mammalian cells. Incorporation of the azide-bearing amino acid azidohomoalanine is unbiased, not toxic, and does not increase protein degradation. As a first demonstration of the method, we report the selective purification and identification of 195 metabolically labeled proteins with multidimensional liquid chromatography in-line with tandem MS. Furthermore, in combination with leucine-based mass tagging, candidates were immediately validated as newly synthesized proteins. The identified proteins, synthesized in a 2-h window, possess a broad range of biochemical properties and span most functional gene ontology categories. This technology makes it possible to address the temporal and spatial characteristics of newly synthesized proteomes in any cell type.
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Proteins within a specific cell type can be uniquely labeled in vivo via BONCAT and isolated from complex tissue for MS-based proteomics.
“Proteins within a specific cell type can be uniquely labeled in vivo via BONCAT (Fig. 2) and isolated from a complex tissue, such as the brain, for MS-based proteomics.”
From Systems-based proteomics to resolve the biology of Alzheimer’s disease beyond amyloid and tau (2021) · cites this paper as [157]
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- Authors
- Dieterich, D. C., Link, A. J., Graumann, J., Tirrell, D. A., & Schuman, E. M.
- Affiliations
- Howard Hughes Medical Institute (US)
- California Institute of Technology (US)
- Corresponding author
- Schuman, Erin M.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2006-06-20
- Volume
- 103
- Issue
- 25
- Pages
- 9482-9487
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1480433
- OpenAlex
- W2157162286
- Cited by
- 874
- References
- 62
- Citations by year
- 2026: 60 · 2025: 61 · 2024: 56 · 2023: 65 · 2022: 49 · 2021: 70 · 2020: 70 · 2019: 47 · 2018: 56 · 2017: 51 · 2016: 53 · 2015: 45 · 2014: 41 · 2013: 25 · 2012: 26
- FWCI
- 7.63
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- National Science Foundation
- Howard Hughes Medical Institute
- U.S. Department of Energy
- California Institute of Technology
- Bundesministerium für Bildung und Forschung
- Topics
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Physical Sciences › Chemistry › Organic Chemistry › Click Chemistry and Applications
- Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
- Keywords
- BONCAT, newly synthesized proteins, protein synthesis, azidohomoalanine, proteome dynamics, mammalian cells
- MeSH terms
- Amino Acids, Azides, Cell Line, Humans, Proteins, Protein Biosynthesis, Molecular Structure
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