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The ATAC and SAGA coactivator complexes assemble co-translationally, but their cellular localization properties and functions are distinct

ABSTRACT: To understand the precise mechanism that guide the formation of multisubunit complexes is of key importance. Nascent proteins can find and bind their interaction partners during their translation, leading to co-translational assembly. Here we demonstrate that the distinct 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. Fully assembled SAGA complex forms in the cytoplasm of mammalian cells and cytoplasmic SAGA acetylates non-histones proteins, before imported in the nucleus. In contrast, ATAC has no cytoplasmic functions as it cannot be detected in the cytoplasm of mammalian cells. However, fully assembled endogenous ATAC complex containing two functional modules forms and functions in the nucleus. Thus, the two related co-activators, ATAC and SAGA, assemble by using co-translational pathways, but their subcellular localization, cytoplasmic detectability and functions are distinct.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell

DISEASE(S): Disease Free

SUBMITTER: Luc Negroni

LAB HEAD: Laszlo Tora

PROVIDER: PXD038695 | Pride | 2023-09-27

REPOSITORIES: Pride

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			Action	DRS
	170418_ES_ech01_rep1.msf	Msf
	170418_ES_ech01_rep1.raw	Raw
	170418_ES_ech01_rep2.msf	Msf
	170418_ES_ech01_rep2.raw	Raw
	170418_ES_ech01_rep3.msf	Msf

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TAF8 MUTATION CAUSES INTELLECUAL DISABILITY, TFIID DISASSEMBLY WITH NO EFFECT ON RNA POLYMERASE II TRANSCRIPTION

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