On the evolution of chaperones and cochaperones and the expansion of proteomes across the Tree of Life.
Adenosine Triphosphate
/ metabolism
Animals
Archaea
/ genetics
Bacteria
/ genetics
Evolution, Molecular
Fungi
/ genetics
Gene Expression
Gene Ontology
HSP70 Heat-Shock Proteins
/ genetics
Mammals
Molecular Sequence Annotation
Phylogeny
Plants
/ genetics
Protein Aggregates
/ genetics
Protein Folding
Protein Isoforms
/ genetics
Proteome
/ genetics
RNA, Messenger
/ genetics
Tree of Life
chaperone network
cochaperones
core chaperones
expansion of proteomes
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
25 05 2021
25 05 2021
Historique:
entrez:
18
5
2021
pubmed:
19
5
2021
medline:
15
12
2021
Statut:
ppublish
Résumé
Across the Tree of Life (ToL), the complexity of proteomes varies widely. Our systematic analysis depicts that from the simplest archaea to mammals, the total number of proteins per proteome expanded ∼200-fold. Individual proteins also became larger, and multidomain proteins expanded ∼50-fold. Apart from duplication and divergence of existing proteins, completely new proteins were born. Along the ToL, the number of different folds expanded ∼5-fold and fold combinations ∼20-fold. Proteins prone to misfolding and aggregation, such as repeat and beta-rich proteins, proliferated ∼600-fold and, accordingly, proteins predicted as aggregation-prone became 6-fold more frequent in mammalian compared with bacterial proteomes. To control the quality of these expanding proteomes, core chaperones, ranging from heat shock proteins 20 (HSP20s) that prevent aggregation to HSP60, HSP70, HSP90, and HSP100 acting as adenosine triphosphate (ATP)-fueled unfolding and refolding machines, also evolved. However, these core chaperones were already available in prokaryotes, and they comprise ∼0.3% of all genes from archaea to mammals. This challenge-roughly the same number of core chaperones supporting a massive expansion of proteomes-was met by 1) elevation of messenger RNA (mRNA) and protein abundances of the ancient generalist core chaperones in the cell, and 2) continuous emergence of new substrate-binding and nucleotide-exchange factor cochaperones that function cooperatively with core chaperones as a network.
Identifiants
pubmed: 34001607
pii: 2020885118
doi: 10.1073/pnas.2020885118
pmc: PMC8166112
pii:
doi:
Substances chimiques
HSP70 Heat-Shock Proteins
0
Protein Aggregates
0
Protein Isoforms
0
Proteome
0
RNA, Messenger
0
Adenosine Triphosphate
8L70Q75FXE
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Informations de copyright
Copyright © 2021 the Author(s). Published by PNAS.
Déclaration de conflit d'intérêts
The authors declare no competing interest.
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