Engineering of ultraID, a compact and hyperactive enzyme for proximity-dependent biotinylation in living cells.
Journal
Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179
Informations de publication
Date de publication:
04 07 2022
04 07 2022
Historique:
received:
02
06
2021
accepted:
20
06
2022
entrez:
5
7
2022
pubmed:
6
7
2022
medline:
7
7
2022
Statut:
epublish
Résumé
Proximity-dependent biotinylation (PDB) combined with mass spectrometry analysis has established itself as a key technology to study protein-protein interactions in living cells. A widespread approach, BioID, uses an abortive variant of the E. coli BirA biotin protein ligase, a quite bulky enzyme with slow labeling kinetics. To improve PDB versatility and speed, various enzymes have been developed by different approaches. Here we present a small-size engineered enzyme: ultraID. We show its practical use to probe the interactome of Argonaute-2 after a 10 min labeling pulse and expression at physiological levels. Moreover, using ultraID, we provide a membrane-associated interactome of coatomer, the coat protein complex of COPI vesicles. To date, ultraID is the smallest and most efficient biotin ligase available for PDB and offers the possibility of investigating interactomes at a high temporal resolution.
Identifiants
pubmed: 35788163
doi: 10.1038/s42003-022-03604-5
pii: 10.1038/s42003-022-03604-5
pmc: PMC9253107
doi:
Substances chimiques
Escherichia coli Proteins
0
Repressor Proteins
0
Biotin
6SO6U10H04
Carbon-Nitrogen Ligases
EC 6.3.-
birA protein, E coli
EC 6.3.4.15
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
657Informations de copyright
© 2022. The Author(s).
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