G-Quadruplexes act as sequence-dependent protein chaperones.
RNA
nucleic acids
protein aggregation
protein folding
proteostasis
Journal
EMBO reports
ISSN: 1469-3178
Titre abrégé: EMBO Rep
Pays: England
ID NLM: 100963049
Informations de publication
Date de publication:
05 10 2020
05 10 2020
Historique:
received:
22
11
2019
revised:
29
07
2020
accepted:
05
08
2020
pubmed:
19
9
2020
medline:
28
4
2021
entrez:
18
9
2020
Statut:
ppublish
Résumé
Maintaining proteome health is important for cell survival. Nucleic acids possess the ability to prevent protein aggregation more efficiently than traditional chaperone proteins. In this study, we explore the sequence specificity of the chaperone activity of nucleic acids. Evaluating over 500 nucleic acid sequences' effects on protein aggregation, we show that the holdase chaperone effect of nucleic acids is sequence-dependent. G-Quadruplexes prevent protein aggregation via quadruplex:protein oligomerization. They also increase the folded protein level of a biosensor in E. coli. These observations contextualize recent reports of quadruplexes playing important roles in aggregation-related diseases, such as fragile X and amyotrophic lateral sclerosis (ALS), and provide evidence that nucleic acids have the ability to modulate the folding environment of E. coli.
Identifiants
pubmed: 32945124
doi: 10.15252/embr.201949735
pmc: PMC7534610
doi:
Substances chimiques
Molecular Chaperones
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
e49735Subventions
Organisme : NIGMS NIH HHS
ID : R00 GM120388
Pays : United States
Informations de copyright
© 2020 The Authors. Published under the terms of the CC BY 4.0 license.
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