ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct.
Cell Rep
; 42(9): 113099, 2023 09 26.
Article
in En
| MEDLINE
| ID: mdl-37682711
ABSTRACT
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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Saccharomyces cerevisiae Proteins
/
Histone Acetyltransferases
Limits:
Animals
Language:
En
Journal:
Cell Rep
Year:
2023
Document type:
Article
Affiliation country:
Francia