Interactions between nascent proteins translated by adjacent ribosomes drive homomer assembly

Author:

Bertolini Matilde1ORCID,Fenzl Kai1ORCID,Kats Ilia1ORCID,Wruck Florian2,Tippmann Frank1ORCID,Schmitt Jaro1ORCID,Auburger Josef Johannes1,Tans Sander23ORCID,Bukau Bernd1ORCID,Kramer Günter1ORCID

Affiliation:

1. Center for Molecular Biology of Heidelberg University (ZMBH) and German Cancer Research Center (DKFZ), DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany.

2. AMOLF, Science Park 104, 1098 XG Amsterdam, Netherlands.

3. Department of Bionanoscience, Delft University of Technology and Kavli Institute of Nanoscience Delft, 2629HZ Delft, Netherlands.

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

Funder

European Research Council

Deutsche Forschungsgemeinschaft

Klaus Tschira Stiftung

Netherlands Organization for Scientific Research

Helmholtz-Gemeinschaft

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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