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Proteomic navigation using proximity-labeling.

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Date
2019-07
ICR Author
Pardo Calvo, Maria Mercedes
Choudhary, Jyoti
Author
Gentzel, M
Pardo, M
Subramaniam, S
Stewart, AF
Choudhary, JS
Type
Journal Article
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Abstract
The identification of bona fide protein-protein interactions and the mapping of proteomes was greatly enhanced by protein tagging for generic affinity purification methods and analysis by mass spectrometry (AP-MS). The high quality of AP-MS data permitted the development of proteomic navigation by sequential tagging of identified interactions. However AP-MS is laborious and limited to relatively high affinity protein-protein interactions. Proximity labeling, first with the biotin ligase BirA, termed BioID, and then with ascorbate peroxidase, termed APEX, permits a greater reach into the proteome than AP-MS enabling both the identification of a wider field and weaker protein-protein interactions. This additional reach comes with the need for stringent controls. Proximity labeling also permits experiments in living cells allowing spatiotemporal investigations of the proteome. Here we discuss proximity labeling with accompanying methodological descriptions for E. coli and mammalian cells.
URI
https://repository.icr.ac.uk/handle/internal/3249
DOI
https://doi.org/10.1016/j.ymeth.2019.03.028
Collections
  • Cancer Biology
Subject
Cell Line
Animals
Escherichia coli
Hydrogen Peroxide
Biotin
Carbon-Nitrogen Ligases
Escherichia coli Proteins
Repressor Proteins
Staining and Labeling
Biotinylation
Protein Interaction Mapping
Proteomics
Mass Spectrometry
Ascorbate Peroxidases
Spatio-Temporal Analysis
Research team
Functional Proteomics Group
Language
eng
Date accepted
2019-03-29
License start date
2019-07
Citation
Methods (San Diego, Calif.), 2019, 164-165 pp. 67 - 72

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