TY  - JOUR
AU  - Bernardini, Andrea
AU  - Mukherjee, Pooja
AU  - Scheer, Elisabeth
AU  - Kamenova, Ivanka
AU  - Antonova, Simona
AU  - Mendoza Sanchez, Paulina Karen
AU  - Yayli, Gizem
AU  - Morlet, Bastien
AU  - Timmers, Hermanus Theodorus Marcus
AU  - Tora, László
TI  - Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID.
JO  - Nature structural & molecular biology
VL  - 30
IS  - 8
SN  - 1545-9993
CY  - London [u.a.]
PB  - Nature Publishing Group
M1  - DKFZ-2023-01323
SP  - 1141-1152
PY  - 2023
N1  - 2023 Aug;30(8):1141-1152
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:37386215
DO  - DOI:10.1038/s41594-023-01026-3
UR  - https://inrepo02.dkfz.de/record/277294
ER  -