Interactions between nascent proteins translated by adjacent ribosomes drive homomer assembly
Matilde Bertolini, Kai Fenzl, Ilia Kats, Florian Wruck, Frank Tippmann, Jaro Schmitt, Josef Johannes Auburger, Sander J. Tans, Bernd Bukau, Günter Krämer
Abstract
Co-co assembly for oligomers Most of the human proteome forms oligomeric protein complexes, but how they assemble is poorly understood. Bertolini et al. used a ribosome-profiling approach to explore the existence of a cotranslational assembly mode based on the interaction of two nascent polypeptides, which they call the “co-co” assembly. Proteome-wide data were used to show whether, when, and how efficiently nascent complex subunits interact. The findings also show that human cells use co-co assembly to produce hundreds of different homo-oligomers. Co-co assembly involving ribosomes translating one messenger RNA may resolve the longstanding question of how cells prevent unwanted interactions between different protein isoforms to efficiently produce functional homo-oligomers. Science , this issue p. 57