ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct.
Fiche publication
Date publication
septembre 2023
Journal
Cell reports
Auteurs
Membres identifiés du Cancéropôle Est :
Mr ESSABRI Karim, Dr TORA Laszlo, Dr NEGRONI Luc, Mr MORLET Bastien
Tous les auteurs :
Yayli G, Bernardini A, Mendoza Sanchez PK, Scheer E, Damilot M, Essabri K, Morlet B, Negroni L, Vincent SD, Timmers HTM, Tora L
Lien Pubmed
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.
Mots clés
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
Référence
Cell Rep. 2023 09 7;42(9):113099