ATAC and SAGA coactivator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct - Archive ouverte HAL Access content directly
Preprints, Working Papers, ... Year : 2023

ATAC and SAGA coactivator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct

Abstract

Summary 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 coactivator complexes, assemble co-translationally in the cytoplasm of mammalian cells. In addition, SAGA complex containing all of its modules forms in the cytoplasm and acetylates non-histones proteins. In contrast, fully assembled ATAC complex cannot be detected in the cytoplasm of mammalian cells. However, endogenous ATAC complex containing two functional modules forms and functions in the nucleus. Thus, the two related coactivators, ATAC and SAGA, assemble by using co-translational pathways, but their subcellular localization, cytoplasmic abundance and functions are distinct.
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Dates and versions

hal-04183090 , version 1 (18-08-2023)

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Gizem Yayli, Andrea Bernardini, Paulina Karen Mendoza Sanchez, Elisabeth Scheer, Mylène Damilot, et al.. ATAC and SAGA coactivator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct. 2023. ⟨hal-04183090⟩
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