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Co-translational assembly of mammalian nuclear multisubunit complexes

Abstract : Cells dedicate significant energy to build proteins often organized in multiprotein assemblies with tightly regulated stoichiometries. As genes encoding subunits assembling in a multisubunit complex are dispersed in the genome of eukaryotes, it is unclear how these protein complexes assemble. Here, we show that mammalian nuclear transcription complexes (TFIID, TREX-2 and SAGA) composed of a large number of subunits, but lacking precise architectural details are built co-translationally. We demonstrate that dimerization domains and their positions in the interacting subunits determine the co-translational assembly pathway (simultaneous or sequential). The lack of co-translational interaction can lead to degradation of the partner protein. Thus, protein synthesis and complex assembly are linked in building mammalian multisubunit complexes, suggesting that co-translational assembly is a general principle in mammalian cells to avoid non-specific interactions and protein aggregation. These findings will also advance structural biology by defining endogenous co-translational building blocks in the architecture of multisubunit complexes.
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Contributor : Stéphane Vincent <>
Submitted on : Monday, June 3, 2019 - 5:07:51 PM
Last modification on : Wednesday, April 29, 2020 - 4:38:03 PM


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Ivanka Kamenova, Pooja Mukherjee, Sascha Conic, Florian Mueller, Farrah El-Saafin, et al.. Co-translational assembly of mammalian nuclear multisubunit complexes. Nature Communications, Nature Publishing Group, 2019, 10 (1), ⟨10.1038/s41467-019-09749-y⟩. ⟨hal-02130219⟩



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