Interactions between nascent proteins translated by adjacent ribosomes drive homomer assembly
Matilde Bertolini (Universität Heidelberg)
Kai Fenzl (Universität Heidelberg)
Ilia Kats (Universität Heidelberg)
Florian Wruck (AMOLF Institute for Atomic and Molecular Physics)
Frank Tippmann (Universität Heidelberg)
Jaro Schmitt (Universität Heidelberg)
Josef Johannes Auburger (Universität Heidelberg)
Sander Tans (TU Delft - Applied Sciences, Kavli institute of nanoscience Delft, AMOLF Institute for Atomic and Molecular Physics)
Bernd Bukau (Universität Heidelberg)
Günter Kramer (Universität Heidelberg)
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Abstract
Accurate assembly of newly synthesized proteins into functional oligomers is crucial for cell activity. In this study, we investigated whether direct interaction of two nascent proteins, emerging from nearby ribosomes (co-co assembly), constitutes a general mechanism for oligomer formation. We used proteome-wide screening to detect nascent chain-connected ribosome pairs and identified hundreds of homomer subunits that co-co assemble in human cells. Interactions are mediated by five major domain classes, among which N-terminal coiled coils are the most prevalent. We were able to reconstitute co-co assembly of nuclear lamin in Escherichia coli, demonstrating that dimer formation is independent of dedicated assembly machineries. Co-co assembly may thus represent an efficient way to limit protein aggregation risks posed by diffusion-driven assembly routes and ensure isoform-specific homomer formation.