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Nascent chain interactions of proximal ribosomes drive homo-oligomer assembly


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 a proteome-wide screen 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.

ORGANISM(S): Escherichia coli Homo sapiens

PROVIDER: GSE151959 | GEO | 2020/12/18

REPOSITORIES: GEO

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