ArticleMolecular cell2019
The Ribosome Cooperates with a Chaperone to Guide Multi-domain Protein Folding.
Article in Molecular cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 107 citations in OpenAlex.
- Quasi-continuous cotranslational compaction and folding of a multidomain protein.Nature communications · 2026Article
- A detailed molecular picture of protein folding during active translation.bioRxiv : the preprint server for biology · 2026Article
- Direct single-molecule visualization of Hsp90-mediated relief of an Hsp70-folding block.Science advances · 2026Article
- Article
- 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
- Multivalent weak contacts shape chaperone-nascent protein interactions.bioRxiv : the preprint server for biology · 2026Article
- Momordicine I induces ER stress and inhibits OSCC by targeting ribosomal proteins.Journal of Zhejiang University. Science. B · 2025Article
- 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
- Pathway regulation mechanism by cotranslational protein folding.Communications chemistry · 2025Article
- Trigger factor accelerates nascent chain compaction and folding.Proceedings of the National Academy of Sciences of the United States of America · 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
- FAIR data for optical tweezers experiments.Biophysical journal · 2025Review
- A ribosome-associating chaperone mediates GTP-driven vectorial folding of nascent eEF1A.Nature communications · 2025Article
- Resolving chaperone-assisted protein folding on the ribosome at the peptide level.Nature structural & molecular biology · 2024Article
- Translation Rates and Protein Folding.Journal of molecular biology · 2024Review
- AutoRNC: An automated modeling program for building atomic models of ribosome-nascent chain complexes.Structure (London, England : 1993) · 2024Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Multi-domain proteins, containing several structural units within a single polypeptide, constitute a large fraction of all proteomes. Co-translational folding is assumed to simplify the conformational search problem for large proteins, but the events leading to correctly folded, functional structures remain poorly characterized. Similarly, how the ribosome and molecular chaperones promote efficient folding remains obscure. Using optical tweezers, we have dissected early folding events of nascent elongation factor G, a multi-domain protein that requires chaperones for folding. The ribosome and the chaperone trigger factor reduce inter-domain misfolding, permitting folding of the N-terminal G-domain. Successful completion of this step is a crucial prerequisite for folding of the next domain. Unexpectedly, co-translational folding does not proceed unidirectionally; emerging unfolded polypeptide can denature an already-folded domain. Trigger factor, but not the ribosome, protects against denaturation. The chaperone thus serves a previously unappreciated function, helping multi-domain proteins overcome inherent challenges during co-translational folding.
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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.