Loss of N-terminal acetyltransferase A activity induces thermally unstable ribosomal proteins and increases their turnover in Saccharomyces cerevisiae.
N-Terminal Acetyltransferases
/ genetics
Saccharomyces cerevisiae
/ metabolism
Ribosomal Proteins
/ genetics
N-Terminal Acetyltransferase A
/ metabolism
Saccharomyces cerevisiae Proteins
/ genetics
Proteome
/ metabolism
Acetylation
Acetyltransferases
/ genetics
N-Terminal Acetyltransferase E
/ metabolism
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
27 07 2023
27 07 2023
Historique:
received:
02
11
2022
accepted:
14
07
2023
medline:
31
7
2023
pubmed:
28
7
2023
entrez:
27
7
2023
Statut:
epublish
Résumé
Protein N-terminal (Nt) acetylation is one of the most abundant modifications in eukaryotes, covering ~50-80 % of the proteome, depending on species. Cells with defective Nt-acetylation display a wide array of phenotypes such as impaired growth, mating defects and increased stress sensitivity. However, the pleiotropic nature of these effects has hampered our understanding of the functional impact of protein Nt-acetylation. The main enzyme responsible for Nt-acetylation throughout the eukaryotic kingdom is the N-terminal acetyltransferase NatA. Here we employ a multi-dimensional proteomics approach to analyze Saccharomyces cerevisiae lacking NatA activity, which causes global proteome remodeling. Pulsed-SILAC experiments reveals that NatA-deficient strains consistently increase degradation of ribosomal proteins compared to wild type. Explaining this phenomenon, thermal proteome profiling uncovers decreased thermostability of ribosomes in NatA-knockouts. Our data are in agreement with a role for Nt-acetylation in promoting stability for parts of the proteome by enhancing the avidity of protein-protein interactions and folding.
Identifiants
pubmed: 37500638
doi: 10.1038/s41467-023-40224-x
pii: 10.1038/s41467-023-40224-x
pmc: PMC10374663
doi:
Substances chimiques
N-Terminal Acetyltransferases
EC 2.3.1.88
Ribosomal Proteins
0
N-Terminal Acetyltransferase A
EC 2.3.1.254
Saccharomyces cerevisiae Proteins
0
Proteome
0
Acetyltransferases
EC 2.3.1.-
N-Terminal Acetyltransferase E
EC 2.3.1.258
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4517Subventions
Organisme : European Research Council
ID : EPIC-XS-823839
Pays : International
Informations de copyright
© 2023. The Author(s).
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