Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID - Archive ouverte HAL Access content directly
Journal Articles Nature Structural and Molecular Biology Year : 2023

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-subunit basal transcription factor TFIID nucleates the RNA polymerase II preinitiation complex at gene promoters. Here, by combining systematic RNA-immunoprecipitation (RIP) experiments, single-molecule imaging, proteomics and structure–function analyses, we show that human TFIID biogenesis occurs co-translationally. We discovered that all protein heterodimerization steps happen during protein synthesis. We identify TAF1—the largest protein in the complex—as a critical factor for TFIID assembly. TAF1 acts as a flexible scaffold that drives the co-translational recruitment of TFIID submodules preassembled in the cytoplasm. Altogether, our data suggest a multistep hierarchical model for TFIID biogenesis that culminates with the co-translational assembly of the complex onto the nascent TAF1 polypeptide. We envision that this assembly strategy could be shared with other large heteromeric protein complexes.
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Dates and versions

hal-04173334 , version 1 (28-07-2023)

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Andrea Bernardini, Pooja Mukherjee, Elisabeth Scheer, Ivanka Kamenova, Simona Antonova, et al.. Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID. Nature Structural and Molecular Biology, 2023, 30 (8), pp.1141-1152. ⟨10.1038/s41594-023-01026-3⟩. ⟨hal-04173334⟩
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