Abstract：
: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.
journal_name
Nat Biotechnoljournal_title
Nature biotechnologyauthors
Branon TC,Bosch JA,Sanchez AD,Udeshi ND,Svinkina T,Carr SA,Feldman JL,Perrimon N,Ting AYdoi
10.1038/nbt.4201subject
Has Abstractpub_date
2018-10-01 00:00:00pages
880-887issue
9eissn
1087-0156issn
1546-1696pii
nbt.4201journal_volume
36pub_type
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