%0 Journal Article
%A Bernardini, Andrea
%A Mukherjee, Pooja
%A Scheer, Elisabeth
%A Kamenova, Ivanka
%A Antonova, Simona
%A Mendoza Sanchez, Paulina Karen
%A Yayli, Gizem
%A Morlet, Bastien
%A Timmers, Hermanus Theodorus Marcus
%A Tora, László
%T Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID.
%J Nature structural & molecular biology
%V 30
%N 8
%@ 1545-9993
%C London [u.a.]
%I Nature Publishing Group
%M DKFZ-2023-01323
%P 1141-1152
%D 2023
%Z 2023 Aug;30(8):1141-1152
%X 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.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:37386215
%R 10.1038/s41594-023-01026-3
%U https://inrepo02.dkfz.de/record/277294