Single-molecule optical tweezers reveals folding steps of the domain swapping mechanism of a protein.
Journal
Biophysical journal
ISSN: 1542-0086
Titre abrégé: Biophys J
Pays: United States
ID NLM: 0370626
Informations de publication
Date de publication:
02 11 2021
02 11 2021
Historique:
received:
14
12
2020
revised:
15
05
2021
accepted:
15
09
2021
pubmed:
24
9
2021
medline:
16
11
2021
entrez:
23
9
2021
Statut:
ppublish
Résumé
Domain swapping is a mechanism of protein oligomerization by which two or more subunits exchange structural elements to generate an intertwined complex. Numerous studies support a diversity of swapping mechanisms in which structural elements can be exchanged at different stages of the folding pathway of a subunit. Here, we used single-molecule optical tweezers technique to analyze the swapping mechanism of the forkhead DNA-binding domain of human transcription factor FoxP1. FoxP1 populates folded monomers in equilibrium with a swapped dimer. We generated a fusion protein linking two FoxP1 domains in tandem to obtain repetitive mechanical folding and unfolding trajectories. Thus, by stretching the same molecule several times, we detected either the independent folding of each domain or the elusive swapping step between domains. We found that a swapped dimer can be formed directly from fully or mostly folded monomer. In this situation, the interaction between the monomers in route to the domain-swapped dimer is the rate-limiting step. This approach is a useful strategy to test the different proposed domain swapping mechanisms for proteins with relevant physiological functions.
Identifiants
pubmed: 34555362
pii: S0006-3495(21)00788-8
doi: 10.1016/j.bpj.2021.09.026
pmc: PMC8595740
pii:
doi:
Substances chimiques
FOXP1 protein, human
0
Forkhead Transcription Factors
0
Macromolecular Substances
0
Proteins
0
Repressor Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4809-4818Informations de copyright
Copyright © 2021 Biophysical Society. Published by Elsevier Inc. All rights reserved.
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