ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct.
CP: Molecular biology
RIP
RNA immunoprecipitation
YEATS2
ZZZ3
biogenesis
co-translation
lysine acetylation
multiprotein complex
non-histone protein
ribosome
single-molecule RNA FISH
transcription regulation
Journal
Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691
Informations de publication
Date de publication:
26 09 2023
26 09 2023
Historique:
received:
03
01
2023
revised:
19
06
2023
accepted:
22
08
2023
medline:
5
10
2023
pubmed:
8
9
2023
entrez:
8
9
2023
Statut:
ppublish
Résumé
To understand the function of multisubunit complexes, it is of key importance to uncover the precise mechanisms that guide their assembly. Nascent proteins can find and bind their interaction partners during their translation, leading to co-translational assembly. Here, we demonstrate that the core modules of ATAC (ADA-two-A-containing) and SAGA (Spt-Ada-Gcn5-acetyltransferase), two lysine acetyl transferase-containing transcription co-activator complexes, assemble co-translationally in the cytoplasm of mammalian cells. In addition, a SAGA complex containing all of its modules forms in the cytoplasm and acetylates non-histone proteins. In contrast, ATAC complex subunits cannot be detected in the cytoplasm of mammalian cells. However, an endogenous ATAC complex containing two functional modules forms and functions in the nucleus. Thus, the two related co-activators, ATAC and SAGA, assemble using co-translational pathways, but their subcellular localization, cytoplasmic abundance, and functions are distinct.
Identifiants
pubmed: 37682711
pii: S2211-1247(23)01110-5
doi: 10.1016/j.celrep.2023.113099
pmc: PMC10591836
mid: NIHMS1933909
pii:
doi:
Substances chimiques
Histone Acetyltransferases
EC 2.3.1.48
Transcription Factors
0
Chromatin
0
Fungal Proteins
0
Saccharomyces cerevisiae Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
113099Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM139564
Pays : United States
Commentaires et corrections
Type : UpdateOf
Informations de copyright
Copyright © 2023 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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