Pulse labeling reveals the tail end of protein folding by proteome profiling.
CP: Molecular biology
heat stress
limited proteolysis
misfolding
protein aggregation
protein folding
protein mass spectrometry
proteomics
proteostasis
pulse SILAC
translation
Journal
Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691
Informations de publication
Date de publication:
19 07 2022
19 07 2022
Historique:
received:
12
04
2021
revised:
18
05
2022
accepted:
23
06
2022
entrez:
20
7
2022
pubmed:
21
7
2022
medline:
23
7
2022
Statut:
ppublish
Résumé
Accurate and efficient folding of nascent protein sequences into their native states requires support from the protein homeostasis network. Herein we probe which newly translated proteins are thermo-sensitive, making them susceptible to misfolding and aggregation under heat stress using pulse-SILAC mass spectrometry. We find a distinct group of proteins that is highly sensitive to this perturbation when newly synthesized but not once matured. These proteins are abundant and highly structured. Notably, they display a tendency to form β sheet secondary structures, have more complex folding topology, and are enriched for chaperone-binding motifs, suggesting a higher demand for chaperone-assisted folding. These polypeptides are also more often components of stable protein complexes in comparison with other proteins. Combining these findings suggests the existence of a specific subset of proteins in the cell that is particularly vulnerable to misfolding and aggregation following synthesis before reaching the native state.
Identifiants
pubmed: 35858568
pii: S2211-1247(22)00898-1
doi: 10.1016/j.celrep.2022.111096
pmc: PMC9893312
mid: NIHMS1864204
pii:
doi:
Substances chimiques
Molecular Chaperones
0
Peptides
0
Proteome
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Research Support, N.I.H., Extramural
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
111096Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM124818
Pays : United States
Organisme : CIHR
ID : PJT 148489
Pays : Canada
Informations de copyright
Copyright © 2022 The Author(s). Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no competing interests.
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