ArticleScientific reports2016
Reversible thermal unfolding of a yfdX protein with chaperone-like activity.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Thr-to-Ala Mutation Leads to a Larger Aromatic Pair and Reduced Packing Density in α1,α3-Helices during Thioredoxin Cold Adaptation.ACS omega · 2024Article
- Elucidating Protein-Ligand Interactions in Cell Lysates Using High-Throughput Hydrogen-Deuterium Exchange Mass Spectrometry with Integrated Protein Thermal Depletion.Analytical chemistry · 2023Article
- Crystal structure and biochemical analysis suggest that YjoB ATPase is a putative substrate-specific molecular chaperone.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Protein Unfolding: Denaturant vs. Force.Biomedicines · 2021Article
- Ecology and Function of the Transmissible Locus of Stress Tolerance in Escherichia coli and Plant-AssociatedmSystems · 2021Article
- Contribution of the Locus of Heat Resistance to Growth and Survival ofMicroorganisms · 2021Article
- PV1 Protein fromInternational journal of molecular sciences · 2020Article
- Thermal unfolding and refolding of a lytic polysaccharide monooxygenase fromRSC advances · 2019Article
- RcsB regulation of the YfdX-mediated acid stress response in Klebsiella pneumoniae CG43S3.PloS one · 2019Article
- Article
- Structural and Physiological Exploration ofFrontiers in microbiology · 2018Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
yfdX proteins are ubiquitously present in a large number of virulent bacteria. A member of this family of protein in E. coli is known to be up-regulated by the multidrug response regulator. Their abundance in such bacteria suggests some important yet unidentified functional role of this protein. Here, we study the thermal response and stability of yfdX protein STY3178 from Salmonella Typhi using circular dichroism, steady state fluorescence, dynamic light scattering and nuclear magnetic resonance experiments. We observe the protein to be stable up to a temperature of 45 °C. It folds back to the native conformation from unfolded state at temperature as high as 80 °C. The kinetic measurements of unfolding and refolding show Arrhenius behavior where the refolding involves less activation energy barrier than that of unfolding. We propose a homology model to understand the stability of the protein. Our molecular dynamic simulation studies on this model structure at high temperature show that the structure of this protein is quite stable. Finally, we report a possible functional role of this protein as a chaperone, capable of preventing DTT induced aggregation of insulin. Our studies will have broader implication in understanding the role of yfdX proteins in bacterial function and virulence.
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