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Efficient proximity labeling in living cells and organisms with TurboID
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Efficient proximity labeling in living cells and organisms with TurboID
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Journal Article
Efficient proximity labeling in living cells and organisms with TurboID
2018
Overview
Protein–protein interactions in cells are rapidly identified with improved proximity labeling methods.
Protein interaction networks and protein compartmentalization underlie all signaling and regulatory processes in cells. Enzyme-catalyzed proximity labeling (PL) has emerged as a new approach to study the spatial and interaction characteristics of proteins in living cells. However, current PL methods require over 18 h of labeling time or utilize chemicals with limited cell permeability or high toxicity. We used yeast display-based directed evolution to engineer two promiscuous mutants of biotin ligase, TurboID and miniTurbo, which catalyze PL with much greater efficiency than BioID or BioID2, and enable 10-min PL in cells with non-toxic and easily deliverable biotin. Furthermore, TurboID extends biotin-based PL to flies and worms.
Publisher
Springer New York,Nature Publishing Group
Subject
/ 14/19
/ 631/61
/ 64/11
/ 64/24
/ 82/58
/ Biomedical Engineering/Biotechnology
/ Biotin
/ Cloning
/ E coli
/ Enzymes
/ Labeling
/ letter
/ Methods
/ Mutation
/ Proteins
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae Proteins - genetics
/ Saccharomyces cerevisiae Proteins - metabolism
/ Toxicity
/ Yeast
