ArticleProtein science : a publication of the Protein Society2017
The ribosome destabilizes native and non-native structures in a nascent multidomain protein.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 64 citations in OpenAlex.
- Multivalent weak contacts shape chaperone-nascent protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Live-cell co-translational folding tracking reveals bidirectional coupling between translation and folding.bioRxiv : the preprint server for biology · 2026Article
- Evolution of the ribosomal exit tunnel through the eyes of the nascent chain.Nucleic acids research · 2026Article
- The Shape of Things to Come: α-Helical Membrane Protein Folding on the Ribosome.Chemical reviews · 2026Review
- Structures of protein folding intermediates on the ribosome.Nature structural & molecular biology · 2026Article
- Cis-Acting Chaperoning by Macromolecular Tethering: A Built-In Layer of Cellular Chaperoning.International journal of molecular sciences · 2026Review
- Multivalent weak contacts shape chaperone-nascent protein interactions.bioRxiv : the preprint server for biology · 2026Article
- Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome.Journal of molecular biology · 2025Review
- The human ribosome modulates multidomain protein biogenesis by delaying cotranslational domain docking.Nature structural & molecular biology · 2025Article
- Cotranslational protein folding through non-native structural intermediates.Science advances · 2025Article
- Arrest Peptide Profiling resolves co-translational folding pathways and chaperone interactions in vivo.Nature communications · 2025Article
- Proteome-wide determinants of co-translational chaperone binding in bacteria.Nature communications · 2025Article
- Article
- Translation Rates and Protein Folding.Journal of molecular biology · 2024Review
- Nascent chains derived from a foldable protein sequence interact with specific ribosomal surface sites near the exit tunnel.Scientific reports · 2024Article
- AutoRNC: An automated modeling program for building atomic models of ribosome-nascent chain complexes.Structure (London, England : 1993) · 2024Article
- How the ribosome shapes cotranslational protein folding.Current opinion in structural biology · 2024Review
- Folding stabilities of ribosome-bound nascent polypeptides probed by mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Is Posttranslational Folding More Efficient Than Refolding from a Denatured State: A Computational Study.The journal of physical chemistry. B · 2023Article
- Co-Translational Folding of Multi-Domain Proteins.Frontiers in molecular biosciences · 2022Review
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Authors and funding
4 authors at 1 institution in 1 country.
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Abstract
Correct folding is a prerequisite for the biological activity of most proteins. Folding has largely been studied using in vitro refolding assays with isolated small, robustly folding proteins. A substantial fraction of all cellular proteomes is composed of multidomain proteins that are often not amenable to this approach, and their folding remains poorly understood. These large proteins likely begin to fold during their synthesis by the ribosome, a large molecular machine that translates the genetic code. The ribosome affects how folding proceeds, but the underlying mechanisms remain largely obscure. We have utilized optical tweezers to study the folding of elongation factor G, a multidomain protein composed of five domains. We find that interactions among unfolded domains interfere with productive folding in the full-length protein. The N-terminal G-domain constitutes an independently folding unit that, upon in vitro refolding, adopts two similar states that correspond to the natively folded and a non-native, possibly misfolded structure. The ribosome destabilizes both of these states, suggesting a mechanism by which terminal misfolding into highly stable, non-native structures is avoided. The ribosome may thus directly contribute to efficient folding by modulating the folding of nascent multidomain proteins.
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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.