ArticlePloS one2013
Hydrophobic collapse of trigger factor monomer in solution.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Multivalent Interactions between Chaperone and Ribosome-Nascent Chain Complex Revealed by High-Speed AFM and MD Simulations.ACS nano · 2025Article
- Structural features of chloroplast trigger factor determined at 2.6 Å resolution.Acta crystallographica. Section D, Structural biology · 2022Article
- The dynamic dimer structure of the chaperone Trigger Factor.Nature communications · 2017Article
- The chaperone toolbox at the single-molecule level: From clamping to confining.Protein science : a publication of the Protein Society · 2017Review
- Conformational dynamics of bacterial trigger factor in apo and ribosome-bound states.PloS one · 2017Article
- The Trigger Factor Chaperone Encapsulates and Stabilizes Partial Folds of Substrate Proteins.PLoS computational biology · 2015Article
- Flexibility of the bacterial chaperone trigger factor in microsecond-timescale molecular dynamics simulations.Biophysical journal · 2013Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Trigger factor (TF) is a chaperone, found in bacterial cells and chloroplasts, that interacts with nascent polypeptide chains to suppress aggregation. While its crystal structure has been resolved, the solution structure and dynamics are largely unknown. We performed multiple molecular dynamics simulations on Trigger factor in solution, and show that its tertiary domains display collective motions hinged about inter-domain linkers with minimal or no loss in secondary structure. Moreover, we find that isolated TF typically adopts a collapsed state, with the formation of domain pairs. This collapse of TF in solution is induced by hydrophobic interactions and stabilised by hydrophilic contacts. To determine the nature of the domain interactions, we analysed the hydrophobicity of the domain surfaces by using the hydrophobic probe method of Acharya et al., as the standard hydrophobicity scales predictions are limited due to the complex environment. We find that the formation of domain pairs changes the hydrophobic map of TF, making the N-terminal and arm2 domain pair more hydrophilic and the head and arm1 domain pair more hydrophobic. These insights into the dynamics and interactions of the TF domains are important to eventually understand chaperone-substrate interactions and chaperone function.
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Registered trials
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