ArticleNature structural & molecular biology2018
Cotranslational protein assembly imposes evolutionary constraints on homomeric proteins.
Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Evolutionary causes and consequences of gene duplication.Nature reviews. Genetics · 2026Review
- Translation efficiency covariation identifies conserved coordination patterns across cell types.Nature biotechnology · 2026Article
- Histone fold domain positioning dictates cotranslational heterodimeric assembly of paralogous TAF12/TAF12L in Candida albicans.The Journal of biological chemistry · 2026Article
- Perturbation of multiprotein complexes in skeletal muscle induces protective proteases in the CNS that degrade pathogenic proteins.npj aging · 2025Article
- Co-translational ribosome pairing enables native assembly of misfolding-prone subunits.Nature communications · 2025Article
- Leveraging protein structural information to improve variant effect prediction.Current opinion in structural biology · 2025Review
- Cellular location shapes quaternary structure of enzymes.Nature communications · 2024Article
- The Effects of Codon Usage on Protein Structure and Folding.Annual review of biophysics · 2024Review
- AutoRNC: An automated modeling program for building atomic models of ribosome-nascent chain complexes.Structure (London, England : 1993) · 2024Article
- Orientationally Averaged Version of the Rotne-Prager-Yamakawa Tensor Provides a Fast but Still Accurate Treatment of Hydrodynamic Interactions in Brownian Dynamics Simulations of Biological Macromolecules.Journal of chemical theory and computation · 2023Article
- Buffering of genetic dominance by allele-specific protein complex assembly.Science advances · 2023Article
- A Short Tale of the Origin of Proteins and Ribosome Evolution.Microorganisms · 2022Review
- Article
- Proteome-wide landscape of solubility limits in a bacterial cell.Scientific reports · 2022Article
- Co-translational assembly orchestrates competing biogenesis pathways.Nature communications · 2022Article
- Heterodimer Formation of the Homodimeric ABC Transporter OpuA.International journal of molecular sciences · 2021Article
- Interactions between nascent proteins translated by adjacent ribosomes drive homomer assembly.Science (New York, N.Y.) · 2021Article
- Solubility-Weighted Index: fast and accurate prediction of protein solubility.Bioinformatics (Oxford, England) · 2020Article
- Designer protein assemblies with tunable phase diagrams in living cells.Nature chemical biology · 2020Article
- Cotranslational folding allows misfolding-prone proteins to circumvent deep kinetic traps.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
20 authors.
Funding
Abstract
Cotranslational protein folding can facilitate rapid formation of functional structures. However, it can also cause premature assembly of protein complexes, if two interacting nascent chains are in close proximity. By analyzing known protein structures, we show that homomeric protein contacts are enriched toward the C termini of polypeptide chains across diverse proteomes. We hypothesize that this is the result of evolutionary constraints for folding to occur before assembly. Using high-throughput imaging of protein homomers in Escherichia coli and engineered protein constructs with N- and C-terminal oligomerization domains, we show that, indeed, proteins with C-terminal homomeric interface residues consistently assemble more efficiently than those with N-terminal interface residues. Using in vivo, in vitro and in silico experiments, we identify features that govern successful assembly of homomers, which have implications for protein design and expression optimization.
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Registered trials
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