ArticleProceedings of the National Academy of Sciences of the United States of America2015
Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 56 citations in OpenAlex.
- Role of Hsp70 chaperone in client-protein folding elucidated by Markov state modeling and NMR restraint-assisted molecular dynamics simulations.Biophysical journal · 2026Article
- Nuclear-Spin Hyperpolarization of Biomolecules by Optically Enhanced NMR at Ultra-High Field.Journal of the Chinese Chemical Society. Zhongguo hua xue hui (Taipei, Taiwan) · 2026Article
- Putative membrane protein Cgl2168 and its variant enhance thermotolerance inSynthetic and systems biotechnology · 2026Article
- Mechanisms and regulation of the Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2026Review
- Structural insights into the disulfide isomerase and chaperone activity of TrbB of the F plasmid type IV secretion system.Current research in structural biology · 2024Article
- Peptide-based molecules for the disruption of bacterial Hsp70 chaperones.Current opinion in chemical biology · 2023Review
- Critical Beginnings: Selective Tuning of Solubility and Structural Accuracy of Newly Synthesized Proteins by the Hsp70 Chaperone System.The journal of physical chemistry. B · 2023Article
- Distribution and solvent exposure of Hsp70 chaperone binding sites across the Escherichia coli proteome.Proteins · 2023Article
- Real-time single-molecule observation of chaperone-assisted protein folding.Science advances · 2022Article
- Computationally-Aided Modeling of Hsp70-Client Interactions: Past, Present, and Future.The journal of physical chemistry. B · 2022Article
- Protein folding in vitro and in the cell: From a solitary journey to a team effort.Biophysical chemistry · 2022Review
- Elucidating the mechanisms underlying protein conformational switching using NMR spectroscopy.Journal of magnetic resonance open · 2022Article
- Structural basis of protein substrate processing by human mitochondrial high-temperature requirement A2 protease.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- An intrinsically disordered nascent protein interacts with specific regions of the ribosomal surface near the exit tunnel.Communications biology · 2021Article
- CheSPI: chemical shift secondary structure population inference.Journal of biomolecular NMR · 2021Article
- Energy landscape remodeling mechanism of Hsp70-chaperone-accelerated protein folding.Biophysical journal · 2021Article
- Studying protein folding in health and disease using biophysical approaches.Emerging topics in life sciences · 2021Article
- Enhanced nuclear-spin hyperpolarization of amino acids and proteins via reductive radical quenchers.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2021Article
- Redefining Molecular Chaperones as Chaotropes.Frontiers in molecular biosciences · 2021Review
- Co-Chaperones in Targeting and Delivery of Misfolded Proteins to the 26S Proteasome.Biomolecules · 2020Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The molecular chaperone heat shock protein 70 (Hsp70) plays a vital role in cellular processes, including protein folding and assembly, and helps prevent aggregation under physiological and stress-related conditions. Although the structural changes undergone by full-length client proteins upon interaction with DnaK (i.e., Escherichia coli Hsp70) are fundamental to understand chaperone-mediated protein folding, these changes are still largely unexplored. Here, we show that multiple conformations of the SRC homology 3 domain (SH3) client protein interact with the ADP-bound form of the DnaK chaperone. Chaperone-bound SH3 is largely unstructured yet distinct from the unfolded state in the absence of DnaK. The bound client protein shares a highly flexible N terminus and multiple slowly interconverting conformations in different parts of the sequence. In all, there is significant structural and dynamical heterogeneity in the DnaK-bound client protein, revealing that proteins may undergo some conformational sampling while chaperone-bound. This result is important because it shows that the surface of the Hsp70 chaperone provides an aggregation-free environment able to support part of the search for the native state.
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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.