RT Journal Article
SR Electronic
T1 Co-translational assembly counteracts promiscuous interactions
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2021.07.13.452229
DO 10.1101/2021.07.13.452229
A1 Maximilian Seidel
A1 Anja Becker
A1 Filipa Pereira
A1 Jonathan J. M. Landry
A1 Nayara Trevisan Doimo de Azevedo
A1 Claudia M. Fusco
A1 Eva Kaindl
A1 Janina Baumbach
A1 Julian D. Langer
A1 Erin M. Schuman
A1 Kiran Raosaheb Patil
A1 Gerhard Hummer
A1 Vladimir Benes
A1 Martin Beck
YR 2021
UL http://biorxiv.org/content/early/2021/07/13/2021.07.13.452229.abstract
AB During the co-translational assembly of protein complexes, a fully synthesized subunit engages with the nascent chain of a newly synthesized interaction partner. Such events are thought to contribute to productive assembly, but their exact physiological relevance remains underexplored. Here, we examined structural motifs contained in nucleoporins for their potential to facilitate co-translational assembly. We experimentally tested candidate structural motifs and identified several previously unknown co-translational interactions. We demonstrate by selective ribosome profiling that domain invasion motifs of beta-propellers, coiled-coils, and short linear motifs act as co-translational assembly domains. Such motifs are often contained in proteins that are members of multiple complexes (moonlighters) and engage with closely related paralogs. Surprisingly, moonlighters and paralogs assembled co-translationally in only one but not all of the relevant assembly pathways. Our results highlight the regulatory complexity of assembly pathways.Competing Interest StatementThe authors have declared no competing interest.