Proteomics

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Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID


ABSTRACT: Large heteromeric multiprotein complexes play pivotal roles at every step of gene expression in eukaryotic cells. Among them, the 20-subunits basal transcription factor TFIID nucleates RNA polymerase II preinitiation complex at gene promoters. Here, by combining systematic RNA-immunoprecipitation experiments, single-molecule imaging, proteomics and structure-function analyses, we show that TFIID is built using co-translational assembly. We discovered that all early steps of TFIID assembly, involving protein heterodimerization, happen during protein synthesis. Strikingly, we identify TAF1 – the largest protein in the complex – as a flexible scaffold subunit that co-translationally recruits preassembled TFIID submodules found populating the cytoplasm of cells. Consequently, TAF1 depletion leads to a cytoplasmic accumulation of TFIID building blocks. Altogether, our data suggest a multistep hierarchical model for TFIID biogenesis that culminates with the co-translational assembly on nascent TAF1 polypeptide, that works as a ‘driver’ subunit. We envision that this assembly strategy could be shared with other large heteromeric protein complexes.

INSTRUMENT(S): Orbitrap Exploris 480, LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Permanent Cell Line Cell

SUBMITTER: Luc Negroni  

LAB HEAD: Laszlo Tora

PROVIDER: PXD036358 | Pride | 2023-07-04

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
211210_AB_Ech01_Rep1.msf Msf
211210_AB_Ech01_Rep1.raw Raw
211210_AB_Ech01_Rep2.msf Msf
211210_AB_Ech01_Rep2.raw Raw
211210_AB_Ech01_Rep3.msf Msf
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