Proximity Dependent Biotinylation: Key Enzymes and Adaptation to Proteomics Approaches.
APEX
BioID
Protein-protein interactions
biotin ligase
cellular organelles
enzymes
mass spectrometry
molecular biology
peroxidase
protein engineering
proximity-dependent biotinylation
Journal
Molecular & cellular proteomics : MCP
ISSN: 1535-9484
Titre abrégé: Mol Cell Proteomics
Pays: United States
ID NLM: 101125647
Informations de publication
Date de publication:
05 2020
05 2020
Historique:
received:
13
01
2020
revised:
25
02
2020
pubmed:
5
3
2020
medline:
5
2
2021
entrez:
5
3
2020
Statut:
ppublish
Résumé
The study of protein subcellular distribution, their assembly into complexes and the set of proteins with which they interact with is essential to our understanding of fundamental biological processes. Complementary to traditional assays, proximity-dependent biotinylation (PDB) approaches coupled with mass spectrometry (such as BioID or APEX) have emerged as powerful techniques to study proximal protein interactions and the subcellular proteome in the context of living cells and organisms. Since their introduction in 2012, PDB approaches have been used in an increasing number of studies and the enzymes themselves have been subjected to intensive optimization. How these enzymes have been optimized and considerations for their use in proteomics experiments are important questions. Here, we review the structural diversity and mechanisms of the two main classes of PDB enzymes: the biotin protein ligases (BioID) and the peroxidases (APEX). We describe the engineering of these enzymes for PDB and review emerging applications, including the development of PDB for coincidence detection (split-PDB). Lastly, we briefly review enzyme selection and experimental design guidelines and reflect on the labeling chemistries and their implication for data interpretation.
Identifiants
pubmed: 32127388
pii: S1535-9476(20)35002-7
doi: 10.1074/mcp.R120.001941
pmc: PMC7196579
pii:
doi:
Substances chimiques
Enzymes
0
Banques de données
PDB
['2EWN', '3EFS', '1OAG']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
757-773Subventions
Organisme : CIHR
ID : FDN 143301
Pays : Canada
Informations de copyright
© 2020 Samavarchi-Tehrani et al.
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