ArticleNature communications2017
The dynamic dimer structure of the chaperone Trigger Factor.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Multivalent Interactions between Chaperone and Ribosome-Nascent Chain Complex Revealed by High-Speed AFM and MD Simulations.ACS nano · 2025Article
- Thermodynamic profiles for cotranslational trigger factor substrate recognition.Science advances · 2024Article
- Structural basis of substrate recognition and allosteric activation of the proapoptotic mitochondrial HtrA2 protease.Nature communications · 2024Article
- Thumb-domain dynamics modulate the functional repertoire of DNA-Polymerase IV (DinB).Nucleic acids research · 2023Article
- Disulfide-Bond-Induced Structural Frustration and Dynamic Disorder in a Peroxiredoxin from MAS NMR.Journal of the American Chemical Society · 2023Article
- Structural features of chloroplast trigger factor determined at 2.6 Å resolution.Acta crystallographica. Section D, Structural biology · 2022Article
- Trigger factor both holds and folds its client proteins.Nature communications · 2022Article
- Article
- Structural basis of DegP protease temperature-dependent activation.Science advances · 2021Article
- Altered ceramide metabolism is a feature in the extracellular vesicle-mediated spread of alpha-synuclein in Lewy body disorders.Acta neuropathologica · 2021Article
- The interactions of molecular chaperones with client proteins: why are they so weak?The Journal of biological chemistry · 2021Review
- Zinc-Dependent Oligomerization ofBiology · 2021Article
- Structural polymorphism and substrate promiscuity of a ribosome-associated molecular chaperone.Magnetic resonance (Gottingen, Germany) · 2021Article
- Redefining Molecular Chaperones as Chaotropes.Frontiers in molecular biosciences · 2021Review
- UvrD helicase-RNA polymerase interactions are governed by UvrD's carboxy-terminal Tudor domain.Communications biology · 2020Article
- Regulation of chaperone function by coupled folding and oligomerization.Science advances · 2020Article
- Inter-domain dynamics in the chaperone SurA and multi-site binding to its outer membrane protein clients.Nature communications · 2020Article
- Nature and Regulation of Protein Folding on the Ribosome.Trends in biochemical sciences · 2019Review
- Thermosensitive PBP2a requires extracellular folding factors PrsA and HtrA1 forCommunications biology · 2019Article
- Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The chaperone Trigger Factor (TF) from Escherichia coli forms a dimer at cellular concentrations. While the monomer structure of TF is well known, the spatial arrangement of this dimeric chaperone storage form has remained unclear. Here, we determine its structure by a combination of high-resolution NMR spectroscopy and biophysical methods. TF forms a symmetric head-to-tail dimer, where the ribosome binding domain is in contact with the substrate binding domain, while the peptidyl-prolyl isomerase domain contributes only slightly to the dimer affinity. The dimer structure is highly dynamic, with the two ribosome binding domains populating a conformational ensemble in the center. These dynamics result from intermolecular in trans interactions of the TF client-binding site with the ribosome binding domain, which is conformationally frustrated in the absence of the ribosome. The avidity in the dimer structure explains how the dimeric state of TF can be monomerized also by weakly interacting clients.
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