Co-Translational Folding of Multi-Domain Proteins.
co-translational folding
inter-domain interactions
multi-domain proteins
optical tweezers
protein misfolding
ribosome
single-molecule methods
Journal
Frontiers in molecular biosciences
ISSN: 2296-889X
Titre abrégé: Front Mol Biosci
Pays: Switzerland
ID NLM: 101653173
Informations de publication
Date de publication:
2022
2022
Historique:
received:
03
02
2022
accepted:
21
03
2022
entrez:
6
5
2022
pubmed:
7
5
2022
medline:
7
5
2022
Statut:
epublish
Résumé
The majority of proteins in nature are composed of multiple domains connected in a single polypeptide. How these long sequences fold into functional structures without forming toxic misfolds or aggregates is poorly understood. Their folding is inextricably linked to protein synthesis and interactions with cellular machinery, making mechanistic studies challenging. Recent progress has revealed critical features of multi-domain protein folding in isolation and in the context of translation by the ribosome. In this review, we discuss challenges and progress in understanding multi-domain protein folding, and highlight how molecular interactions shape folding and misfolding pathways. With the development of new approaches and model systems, the stage is now set for mechanistically exploring the folding of large multi-domain proteins.
Identifiants
pubmed: 35517860
doi: 10.3389/fmolb.2022.869027
pii: 869027
pmc: PMC9065291
doi:
Types de publication
Journal Article
Review
Langues
eng
Pagination
869027Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM121567
Pays : United States
Informations de copyright
Copyright © 2022 Rajasekaran and Kaiser.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. The handling editor declared a shared affiliation with the authors NR/CK at time of review.
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