ArticleNature communications2022
Trigger factor both holds and folds its client proteins.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 50 citations in OpenAlex.
- Quasi-continuous cotranslational compaction and folding of a multidomain protein.Nature communications · 2026Article
- Enzyme-Inspired Design of Redox-Active Molecules for Promotion of Oxidative Protein Folding.Chembiochem : a European journal of chemical biology · 2026Review
- Hydrogen/deuterium exchange mass spectrometry analysis of ribosome-nascent chain complexes to study protein biogenesis at the peptide level.Nature protocols · 2026Article
- Predicting the protein interaction landscape of a free-living bacterium with pooled-AlphaFold3.Molecular systems biology · 2026Article
- Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis.Molecular & cellular proteomics : MCP · 2026Article
- Multivalent weak contacts shape chaperone-nascent protein interactions.bioRxiv : the preprint server for biology · 2026Article
- Chaperone dependency during biogenesis does not correlate with chaperone dependency during refolding.Molecular systems biology · 2026Article
- Lessons in longevity from blood stem cells under protein stress.Trends in cell biology · 2026Review
- Effect of the Bacterial Chaperones SecB and Trigger Factor (TF) on the Folding Dynamics and In Vitro Translocation of Cytoplasmic and Secretory Model Proteins.International journal of molecular sciences · 2025Article
- On-demand insulin manufacturing using cell-free systems with an "on-column" conversion approach.New biotechnology · 2025Article
- Mechanistic Insights into Protein Biogenesis and Maturation on the Ribosome.Journal of molecular biology · 2025Review
- Chaperone Dependency during Primary Protein Biogenesis Does Not Correlate with Chaperone Dependency duringbioRxiv : the preprint server for biology · 2025Article
- Proteome-wide determinants of co-translational chaperone binding in bacteria.Nature communications · 2025Article
- Surfing in the storm: how Paraburkholderia xenovorans thrives under stress during biodegradation of toxic aromatic compounds and other stressors.FEMS microbiology reviews · 2025Review
- Making Proteins with Electricity.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Beyond Misfolding: A New Paradigm for the Relationship Between Protein Folding and Aggregation.International journal of molecular sciences · 2024Review
- The Effects of the Combined Co-Expression of GroEL/ES and Trigger Factor Chaperones on Orthopoxvirus Phospholipase F13 Production inBiotech (Basel (Switzerland)) · 2024Article
- Resolving chaperone-assisted protein folding on the ribosome at the peptide level.Nature structural & molecular biology · 2024Article
- Article
- Structure-guided design and evaluation of CRM197-scaffolded vaccine targeting GnRH for animal immunocastration.Applied microbiology and biotechnology · 2024Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
ATP-independent chaperones like trigger factor are generally assumed to play passive roles in protein folding by acting as holding chaperones. Here we show that trigger factor plays a more active role. Consistent with a role as an aggregation inhibiting chaperone, we find that trigger factor rapidly binds to partially folded glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and prevents it from non-productive self-association by shielding oligomeric interfaces. In the traditional view of holding chaperone action, trigger factor would then be expected to transfer its client to a chaperone foldase system for complete folding. Unexpectedly, we noticed that GAPDH folds into a monomeric but otherwise rather native-like intermediate state while trigger factor-bound. Upon release from trigger factor, the mostly folded monomeric GAPDH rapidly self-associates into its native tetramer and acquires enzymatic activity without needing additional folding factors. The mechanism we propose here for trigger factor bridges the holding and folding activities of chaperone function.
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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.