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

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Bernardini, Andrea | Mukherjee, Pooja | Scheer, Elisabeth | Kamenova, Ivanka | Antonova, Simona | Mendoza Sanchez, Paulina Karen | Yayli, Gizem | Morlet, Bastien | Timmers, H.T. Marc | Tora, László

Edité par CCSD ; Nature Publishing Group -

International audience. 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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