ArticleeLife2022
Large protein complex interfaces have evolved to promote cotranslational assembly.
Article in eLife, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 33 citations in OpenAlex.
- ModelArchive: A Deposition Database for Computational Macromolecular Structural Models.Journal of molecular biology · 2025Article
- KIF1C activates and extends dynein movement through the FHF cargo adapter.Nature structural & molecular biology · 2025Article
- RING 4.0: faster residue interaction networks with novel interaction types across over 35,000 different chemical structures.Nucleic acids research · 2024Article
- Evidence for dual targeting control of Arabidopsis 6-phosphogluconate dehydrogenase isoforms by N-terminal phosphorylation.Journal of experimental botany · 2024Article
- Diverging co-translational protein complex assembly pathways are governed by interface energy distribution.Nature communications · 2024Article
- ATAC and SAGA co-activator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct.Cell reports · 2023Article
- ATAC and SAGA coactivator complexes utilize co-translational assembly, but their cellular localization properties and functions are distinct.bioRxiv : the preprint server for biology · 2023Article
- Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID.Nature structural & molecular biology · 2023Article
- Buffering of genetic dominance by allele-specific protein complex assembly.Science advances · 2023Article
- Benefits of co-translational complex assembly for cellular fitness.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Hierarchical TAF1-dependent co-translational assembly of the basal transcription factor TFIID.bioRxiv : the preprint server for biology · 2023Article
- Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Assembly pathways of protein complexes should be precise and efficient to minimise misfolding and unwanted interactions with other proteins in the cell. One way to achieve this efficiency is by seeding assembly pathways during translation via the cotranslational assembly of subunits. While recent evidence suggests that such cotranslational assembly is widespread, little is known about the properties of protein complexes associated with the phenomenon. Here, using a combination of proteome-specific protein complex structures and publicly available ribosome profiling data, we show that cotranslational assembly is particularly common between subunits that form large intermolecular interfaces. To test whether large interfaces have evolved to promote cotranslational assembly, as opposed to cotranslational assembly being a non-adaptive consequence of large interfaces, we compared the sizes of first and last translated interfaces of heteromeric subunits in bacterial, yeast, and human complexes. When considering all together, we observe the N-terminal interface to be larger than the C-terminal interface 54% of the time, increasing to 64% when we exclude subunits with only small interfaces, which are unlikely to cotranslationally assemble. This strongly suggests that large interfaces have evolved as a means to maximise the chance of successful cotranslational subunit binding.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.