ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct.
ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct.
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DOI:
10.1016/j.celrep.2023.113099
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发表时间:
2023-09-26
期刊:
影响因子:
8.8
通讯作者:
中科院分区:
文献类型:
--
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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. Yayli et al. find that modules of human ATAC (ADA-two-A-containing) and SAGA (Spt-Ada-Gcn5-acetyltransferase) transcriptional co-activator complexes assemble co-translationally in the cytoplasm. They describe that fully assembled SAGA has cytoplasmic acetylation functions. In contrast, the ATAC co-activator complex cannot be detected in the cytoplasm, only in the nucleus.
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